[English] 日本語
Yorodumi
- EMDB-41200: Human cytomegalovirus portal vertex, virion configuration 2 (VC2) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-41200
TitleHuman cytomegalovirus portal vertex, virion configuration 2 (VC2)
Map dataPost-processed map used for real space refinement.
Sample
  • Virus: Human herpesvirus 5 strain AD169
    • Protein or peptide: Large tegument protein deneddylase
    • Protein or peptide: Capsid vertex component 2
    • Protein or peptide: Capsid vertex component 1
    • Protein or peptide: Major capsid protein
    • Protein or peptide: Small capsomere-interacting protein
    • Protein or peptide: Triplex capsid protein 1
    • Protein or peptide: Triplex capsid protein 2
    • Protein or peptide: Large structural phosphoprotein
Keywordstegument / portal / DNA packaging / intracellular transport / VIRUS
Function / homology
Function and homology information


host cell viral assembly compartment / T=16 icosahedral viral capsid / viral tegument / viral DNA genome packaging / viral capsid assembly / host cell cytoplasmic vesicle / chromosome organization / viral release from host cell / viral process / viral penetration into host nucleus ...host cell viral assembly compartment / T=16 icosahedral viral capsid / viral tegument / viral DNA genome packaging / viral capsid assembly / host cell cytoplasmic vesicle / chromosome organization / viral release from host cell / viral process / viral penetration into host nucleus / viral capsid / symbiont-mediated perturbation of host ubiquitin-like protein modification / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / host cell cytoplasm / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / host cell perinuclear region of cytoplasm / symbiont entry into host cell / host cell nucleus / structural molecule activity / proteolysis / DNA binding
Similarity search - Function
Herpesvirus UL11/UL32 / Small capsid protein, Herpesviridae / Herpesvirus large structural phosphoprotein UL32 / Small capsid protein of Herpesviridae / Large tegument protein deneddylase / Herpesvirus tegument ubiquitin-specific protease (htUSP) domain profile. / Herpesvirus large tegument protein, USP domain / Herpesvirus tegument protein, N-terminal conserved region / Herpesvirus capsid vertex component 1 / Herpesvirus UL17 protein ...Herpesvirus UL11/UL32 / Small capsid protein, Herpesviridae / Herpesvirus large structural phosphoprotein UL32 / Small capsid protein of Herpesviridae / Large tegument protein deneddylase / Herpesvirus tegument ubiquitin-specific protease (htUSP) domain profile. / Herpesvirus large tegument protein, USP domain / Herpesvirus tegument protein, N-terminal conserved region / Herpesvirus capsid vertex component 1 / Herpesvirus UL17 protein / Herpesvirus UL25 / Herpesvirus UL25 family / Herpesvirus capsid protein 2 / Herpesvirus capsid shell protein 1 / Herpesvirus VP23 like capsid protein / Herpesvirus capsid shell protein VP19C / Herpesvirus major capsid protein / Herpesvirus major capsid protein, upper domain superfamily / Herpes virus major capsid protein / Papain-like cysteine peptidase superfamily
Similarity search - Domain/homology
Large structural phosphoprotein / Capsid vertex component 2 / Triplex capsid protein 2 / Major capsid protein / Triplex capsid protein 1 / Large tegument protein deneddylase / Capsid vertex component 1 / Small capsomere-interacting protein
Similarity search - Component
Biological speciesHuman herpesvirus 5 strain AD169
Methodsingle particle reconstruction / cryo EM / Resolution: 3.27 Å
AuthorsJih J / Liu YT / Liu W / Zhou H
Funding support United States, 9 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)DE028583 United States
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)T32AR071307 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)P30 AI152501 United States
James B. Pendleton Charitable Trust (to the UCLA AIDS Institute) United States
McCarthy Family Foundation (to the UCLA AIDS Institute) United States
National Institutes of Health/Office of the Director1S10RR23057 United States
National Institutes of Health/Office of the Director1S10OD018111 United States
National Science Foundation (NSF, United States)DBI-1338135 United States
National Science Foundation (NSF, United States)DMR-1548924 United States
CitationJournal: Sci Adv / Year: 2024
Title: The incredible bulk: Human cytomegalovirus tegument architectures uncovered by AI-empowered cryo-EM.
Authors: Jonathan Jih / Yun-Tao Liu / Wei Liu / Z Hong Zhou /
Abstract: The compartmentalization of eukaryotic cells presents considerable challenges to the herpesvirus life cycle. The herpesvirus tegument, a bulky proteinaceous aggregate sandwiched between ...The compartmentalization of eukaryotic cells presents considerable challenges to the herpesvirus life cycle. The herpesvirus tegument, a bulky proteinaceous aggregate sandwiched between herpesviruses' capsid and envelope, is uniquely evolved to address these challenges, yet tegument structure and organization remain poorly characterized. We use deep-learning-enhanced cryogenic electron microscopy to investigate the tegument of human cytomegalovirus virions and noninfectious enveloped particles (NIEPs; a genome packaging-aborted state), revealing a portal-biased tegumentation scheme. We resolve atomic structures of portal vertex-associated tegument (PVAT) and identify multiple configurations of PVAT arising from layered reorganization of pUL77, pUL48 (large tegument protein), and pUL47 (inner tegument protein) assemblies. Analyses show that pUL77 seals the last-packaged viral genome end through electrostatic interactions, pUL77 and pUL48 harbor a head-linker-capsid-binding motif conducive to PVAT reconfiguration, and pUL47/48 dimers form 45-nm-long filaments extending from the portal vertex. These results provide a structural framework for understanding how herpesvirus tegument facilitates and evolves during processes spanning viral genome packaging to delivery.
History
DepositionJul 6, 2023-
Header (metadata) releaseMar 6, 2024-
Map releaseMar 6, 2024-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

Downloads & links

-
Map

FileDownload / File: emd_41200.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationPost-processed map used for real space refinement.
Voxel sizeX=Y=Z: 1.36 Å
Density
Contour LevelBy AUTHOR: 0.016
Minimum - Maximum-0.04707575 - 0.065917134
Average (Standard dev.)0.00013254075 (±0.005175143)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 489.6 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Additional map: Primary map.

Fileemd_41200_additional_1.map
AnnotationPrimary map.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half map 2.

Fileemd_41200_half_map_1.map
AnnotationHalf map 2.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Half map: Half map 1.

Fileemd_41200_half_map_2.map
AnnotationHalf map 1.
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

-
Sample components

-
Entire : Human herpesvirus 5 strain AD169

EntireName: Human herpesvirus 5 strain AD169
Components
  • Virus: Human herpesvirus 5 strain AD169
    • Protein or peptide: Large tegument protein deneddylase
    • Protein or peptide: Capsid vertex component 2
    • Protein or peptide: Capsid vertex component 1
    • Protein or peptide: Major capsid protein
    • Protein or peptide: Small capsomere-interacting protein
    • Protein or peptide: Triplex capsid protein 1
    • Protein or peptide: Triplex capsid protein 2
    • Protein or peptide: Large structural phosphoprotein

-
Supramolecule #1: Human herpesvirus 5 strain AD169

SupramoleculeName: Human herpesvirus 5 strain AD169 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 10360 / Sci species name: Human herpesvirus 5 strain AD169 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: Yes / Virus empty: No
Host (natural)Organism: Homo sapiens (human)
Virus shellShell ID: 1 / Name: Virion capsid / T number (triangulation number): 16

-
Macromolecule #1: Large tegument protein deneddylase

MacromoleculeName: Large tegument protein deneddylase / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: ubiquitinyl hydrolase 1
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 253.541141 KDa
SequenceString: MKVTQASCHQ GDIARFGARA GNQCVCNGIM FLHALHLGGT SAVLQTEALD AIMEEGARLD ARLERELQKK LPAGGRLPVY RLGDEVPRR LESRFGRTVH ALSRPFNGTT ETCDLDGYMC PGIFDFLRYA HAKPRPTYVL VTVNSLARAV VFTEDHMLVF D PHSSAECH ...String:
MKVTQASCHQ GDIARFGARA GNQCVCNGIM FLHALHLGGT SAVLQTEALD AIMEEGARLD ARLERELQKK LPAGGRLPVY RLGDEVPRR LESRFGRTVH ALSRPFNGTT ETCDLDGYMC PGIFDFLRYA HAKPRPTYVL VTVNSLARAV VFTEDHMLVF D PHSSAECH NAAVYHCEGL HQVLMVLTGF GVQLSPAFYY EALFLYMLDV ATVPEAEIAA RLVSTYRDRD IDLTGVVRES AD TAATTTT AAPSLPPLPD PIVDPGCPPG VAPSIPVYDP SSSPKKTPEK RRKDLSGSKH GGKKKPPSTT SKTLATASSS PSA IAAASS SSAVPPSYSC GEGALPALGR YQQLVDEVEQ ELKALTLPPL PANTSAWTLH AAGTESGANA ATATAPSFDE AFLT DRLQQ LIIHAVNQRS CLRRPCGPQS AAQQAVRAYL GLSKKLDAFL LNWLHHGLDL QRMHDYLSHK TTKGTYSTLD RALLE KMQV VFDPYGRQHG PALIAWVEEM LRYVESKPTN ELSQRLQRFV TKRPMPVSDS FVCLRPVDFQ RLTQVIEQRR RVLQRQ REE YHGVYEHLAG LITSIDIHDL DASDLNRREI LKALQPLDDN AKQELFRLGN AKMLELQMDL DRLSTQLLTR VHNHILN GF LPVEDLKQME RVVEQVLRLF YDLRDLKLCD GSYEEGFVVI REQLSYLMTG TVRDNVPLLQ EILQLRHAYQ QATQQNEG R LTQIHDLLHV IETLVRDPGS RGSALTLALV QEQLAQLEAL GGLQLPEVQQ RLQNAQLALS RLYEEEEETQ RFLDGLSYD DPPNEQTIKR HPQLREMLRR DEQTRLRLIN AVLSMFHTLV MRLARDESPR PTFFDAVSLL LQQLPPDSHE REDLRAANAT YAQMVKKLE QIEKAGTGAS EKRFQALREL VYFFRNHEYF FQHMVGRLGV GPQVTELYER YQHEMEEQHL ERLEREWQEE A GKLTVTSV EDVQRVLARA PSHRVMHQMQ QTLTTKMQDF LDKEKRKQEE QQRQLLDGYQ KKVQQDLQRV VDAVKGEMLS TI PHQPLEA TLELLLGLDQ RAQPLLDKFN QDLLSALQQL SKKLDGRINE CLHGVLTGDV ERRCHPHREA AMQTQASLNH LDQ ILGPQL LIHETQQALQ HAVHQAQFIE KCQQGDPTTA ITGSEFEGDF ARYRSSQQKM EEQLQETRQQ MTETSERLDR SLRQ DPGSS SVTRVPEKPF KGQELAGRIT PPPADFQQPV FKTLLDQQAD AARKALSDEA DLLNQKVQTQ LRQRDEQLST AQNLW TDLV TRHKMSGGLD VTTPDAKALM EKPLETLREL LGKATQQLPY LSAERTVRWM LAFLEEALAQ ITADPTHPHH GSRTHY RNL QQQAVESAVT LAHQIEQNAA CENFIAQHQE ATANGASTPR VDMVQAVEAV WQRLEPGRVA GGAARHQKVQ ELLQRLG QT LGDLELQETL ATEYFALLHG IQTFSYGLDF RSQLEKIRDL RTRFAELAKR RGTRLSNEGV LPNPRKPQAT TSLGAFTR G LNALERHVQL GHQYLLNKLN GSSLVYRLED IPSVLPATHE TDPALIMRDR LRRLCFARHH DTFLEVVDVF GMRQIVTQA GEPIHLVTDY GNVAFKYLAL RDDGRPLAWR RRCSGGGLKN VVTTRYKAIT VAVAVCQTLR TFWPQISQYD LRPYLTQHQS HTHPAETHT LHNLKLFCYL VSTAWHQRID TQQELTAADR VGSGEGGDVG EQRPGRGTVL RLSLQEFCVL IAALYPEYIY T VLKYPVQM SLPSLTAHLH QDVIHAVVNN THKMPPDHLP EQVKAFCITP TQWPAMQLNK LFWENKLVQQ LCQVGPQKST PP LGKLWLY AMATLVFPQD MLQCLWLELK PQYAETYASV SELVQTLFQI FTQQCEMVTE GYTQPQLPTG EPVLQMIRVP RQD TTTTDT NTTTEPGLLD VFIQTETALD YALGSWLFGI PVCLGVHVAD LLKGQRILVA RHLEYTSRDR DFLRIQRSRD LNLS QLLQD TWTETPLEHC WLQAQIRRLR DYLRFPTRLE FIPLVIYNAQ DHTVVRVLRP PSTFEQDHSR LVLDEAFPTF PLYDQ DDNS SADNIAASGA APTPPVPFNR VPVNIQFLRE NPPPIARVQQ PPRRHRHRAA AAADDDGQID HVQDDTSRTA DSALVS TAF GGSVFQENRL GETPLCRDEL VAVAPGAAST SFASPPITVL TQNVLSALEI LRLVRLDLRQ LAQSVQDTIQ HMRFLYL L

UniProtKB: Large tegument protein deneddylase

-
Macromolecule #2: Capsid vertex component 2

MacromoleculeName: Capsid vertex component 2 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 71.26957 KDa
SequenceString: MSLLHTFWRL PVAVFFEPHE ENVLRCPERV LRRLLEDAAV TMRGGGWRED VLMDRVRKRY LRQELRDLGH RVQTYCEDLE GRVSEAEAL LNQQCELDEG PSPRTLLQPP CRPRSSSPGT GVAGASAVPH GLYSRHDAIT GPAAAPSDVV APSDAVAASA A AGASSTWL ...String:
MSLLHTFWRL PVAVFFEPHE ENVLRCPERV LRRLLEDAAV TMRGGGWRED VLMDRVRKRY LRQELRDLGH RVQTYCEDLE GRVSEAEAL LNQQCELDEG PSPRTLLQPP CRPRSSSPGT GVAGASAVPH GLYSRHDAIT GPAAAPSDVV APSDAVAASA A AGASSTWL AQCAERPLPG NVPSYFGITQ NDPFIRFHTD FRGEVVNTMF ENASTWTFSF GIWYYRLKRG LYTQPRWKRV YH LAQMDNF SISQELLLGV VNALENVTVY PTYDCVLSDL EAAACLLAAY GHALWEGRDP PDSVATVLGE LPQLLPRLAD DVS REIAAW EGPVAAGNNY YAYRDSPDLR YYMPLSGGRH YHPGTFDRHV LVRLFHKRGV IQHLPGYGTI TEELVQERLS GQVR DDVLS LWSRRLLVGK LGRDVPVFVH EQQYLRSGLT CLAGLLLLWK VTNADSVFAP RTGKFTLADL LGSDAVAGGG LPGGR AGGE EEGYGGRHGR VRNFEFLVRY YIGPWYARDP AVTLSQLFPG LALLAVTESV RSGWDPSRRE DSAGGGDGGG AVLMQL SKS NPVADYMFAQ SSKQYGDLRR LEVHDALLFH YEHGLGRLLS VTLPRHRVST LGSSLFNVND IYELLYFLVL GFLPSVA VL

UniProtKB: Capsid vertex component 2

-
Macromolecule #3: Capsid vertex component 1

MacromoleculeName: Capsid vertex component 1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 68.567211 KDa
SequenceString: METHLYSDLA FEARFADDEQ LPLHLVLDQE VLSNEEAETL RYVYYRNVDS AGRSTGRAPG GDEDDAPASD DAEDAVGGDR AFDRERRTW QRACFRVLPR PLELLDYLRQ SGLTVTLEKE QRVRMFYAVF TTLGLRCPDN RLSGAQTLHL RLVWPDGSYR D WEFLARDL ...String:
METHLYSDLA FEARFADDEQ LPLHLVLDQE VLSNEEAETL RYVYYRNVDS AGRSTGRAPG GDEDDAPASD DAEDAVGGDR AFDRERRTW QRACFRVLPR PLELLDYLRQ SGLTVTLEKE QRVRMFYAVF TTLGLRCPDN RLSGAQTLHL RLVWPDGSYR D WEFLARDL LREEMEANKR DRQHQLATTT NHRRRGGLRN NLDNGSDRRL PEAAVASLET AVSTPFFEIP NGAGTSSANG DG RFSNLEQ RVARLLRGDE EFIYHAGPLE PPSKIRGHEL VQLRLDVNPD LMYATDPHDR DEVARTDEWK GAGVSRLREV WDV QHRVRL RVLWYVNSFW RSRELSYDDH EVELYRALDA YRARIAVEYV LIRAVRDEIY AVLRRDGGAL PQRFACHVSR NMSW RVVWE LCRHALALWM DWADVRSCII KALTPRLSRG AAAAAQRARR QRERSAPKPQ ELLFGPRNES GPPAEQTWYA DVVRC VRAQ VDLGVEVRAA RCPRTGLWIV RDRRGRLRRW LSQPEVCVLY VTPDLDFYWV LPGGFAVSSR VTLHGLAQRA LRDRFQ NFE AVLARGMHVE AGRQEPETPR VSGRRLPFDD L

UniProtKB: Capsid vertex component 1

-
Macromolecule #4: Major capsid protein

MacromoleculeName: Major capsid protein / type: protein_or_peptide / ID: 4 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 154.048906 KDa
SequenceString: MENWSALELL PKVGIPTDFL THVKTSAGEE MFEALRIYYG DDPERYNIHF EAIFGTFCNR LEWVYFLTSG LAAAAHAIKF HDLNKLTTG KMLFHVQVPR VASGAGLPTS RQTTIMVTKY SEKSPITIPF ELSAACLTYL RETFEGTILD KILNVEAMHT V LRALKNTA ...String:
MENWSALELL PKVGIPTDFL THVKTSAGEE MFEALRIYYG DDPERYNIHF EAIFGTFCNR LEWVYFLTSG LAAAAHAIKF HDLNKLTTG KMLFHVQVPR VASGAGLPTS RQTTIMVTKY SEKSPITIPF ELSAACLTYL RETFEGTILD KILNVEAMHT V LRALKNTA DAMERGLIHS FLQTLLRKAP PYFVVQTLVE NATLARQALN RIQRSNILQS FKAKMLATLF LLNRTRDRDY VL KFLTRLA EAATDSILDN PTTYTTSSGA KISGVMVSTA NVMQIIMSLL SSHITKETVS APATYGNFVL SPENAVTAIS YHS ILADFN SYKAHLTSGQ PHLPNDSLSQ AGAHSLTPLS MDVIRLGEKT VIMENLRRVY KNTDTKDPLE RNVDLTFFFP VGLY LPEDR GYTTVESKVK LNDTVRNALP TTAYLLNRDR AVQKIDFVDA LKTLCHPVLH EPAPCLQTFT ERGPPSEPAM QRLLE CRFQ QEPMGGAARR IPHFYRVRRE VPRTVNEMKQ DFVVTDFYKV GNITLYTELH PFFDFTHCQE NSETVALCTP RIVIGN LPD GLAPGPFHEL RTWEIMEHMR LRPPPDYEET LRLFKTTVTS PNYPELCYLV DVLVHGNVDA FLLIRTFVAR CIVNMFH TR QLLVFAHSYA LVTLIAEHLA DGALPPQLLF HYRNLVAVLR LVTRISALPG LNNGQLAEEP LSAYVNALHD HRLWPPFV T HLPRNMEGVQ VVADRQPLNP ANIEARHHGV SDVPRLGAMD ADEPLFVDDY RATDDEWTLQ KVFYLCLMPA MTNNRACGL GLNLKTLLVD LFYRPAFLLM PAATAVSTSG TTSKESTSGV TPEDSIAAQR QAVGEMLTEL VEDVATDAHT PLLQACRELF LAVQFVGEH VKVLEVRAPL DHAQRQGLPD FISRQHVLYN GCCVVTAPKT LIEYSLPVPF HRFYSNPTIC AALSDDIKRY V TEFPHYHR HDGGFPLPTA FAHEYHNWLR SPFSRYSATC PNVLHSVMTL AAMLYKISPV SLVLQTKAHI HPGFALTAVR TD TFEVDML LYSGKSCTSV IINNPIVTKE ERDISTTYHV TQNINTVDMG LGYTSNTCVA YVNRVRTDMG VRVQDLFRVF PMN VYRHDE VDRWIRHAAG VERPQLLDTE TISMLTFGSM SERNAAATVH GQKAACELIL TPVTMDVNYF KIPNNPRGRA SCML AVDPY DTEAATKAIY DHREADAQTF AATHNPWASQ AGCLSDVLYN TRHRERLGYN SKFYSPCAQY FNTEEIIAAN KTLFK TIDE YLLRAKDCIR GDTDTQYVCV EGTEQLIENP CRLTQEALPI LSTTTLALME TKLKGGAGAF ATSETHFGNY VVGEII PLQ QSMLFNS

UniProtKB: Major capsid protein

-
Macromolecule #5: Small capsomere-interacting protein

MacromoleculeName: Small capsomere-interacting protein / type: protein_or_peptide / ID: 5 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 8.495924 KDa
SequenceString:
MSNTAPGPTV ANKRDEKHRH VVNVVLELPT EISEATHPVL ATMLSKYTRM SSLFNDKCAF KLDLLRMVAV SRTRR

UniProtKB: Small capsomere-interacting protein

-
Macromolecule #6: Triplex capsid protein 1

MacromoleculeName: Triplex capsid protein 1 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 33.07127 KDa
SequenceString: MDARAVAKRP RDPADEDNEL VTALKAKREV NTISVRYLYH ADHQALTARF FVPEGLVEFE AQPGALLIRM ETGCDSPRHL YISLYLLGI RASNVSASTR CLLESVYTAS AARAALQWLD LGPHLLHRRL ETLGCVKTVS LGITSLLTCV MRGYLYNTLK T EVFALMIP ...String:
MDARAVAKRP RDPADEDNEL VTALKAKREV NTISVRYLYH ADHQALTARF FVPEGLVEFE AQPGALLIRM ETGCDSPRHL YISLYLLGI RASNVSASTR CLLESVYTAS AARAALQWLD LGPHLLHRRL ETLGCVKTVS LGITSLLTCV MRGYLYNTLK T EVFALMIP KDMYLTWEET RGRLQYVYLI IVYDYDGPET RPGIYVLTSS IAHWQTLVDV ARGKFARERC SFVNRRITRP RQ IPLCTGV IQKLGWCLAD DIHTSFLVHK ELKLSVVRLD NFSVELGDFR EFV

UniProtKB: Triplex capsid protein 1

-
Macromolecule #7: Triplex capsid protein 2

MacromoleculeName: Triplex capsid protein 2 / type: protein_or_peptide / ID: 7 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 34.63575 KDa
SequenceString: MAAMEANIFC TFDHKLSIAD VGKLTKLVAA VVPIPQRLHL IKHYQLGLHQ FVDHTRGYVR LRGLLRNMTL TLMRRVEGNQ ILLHVPTHG LLYTVLNTGP VTWEKGDALC VLPPLFHGPL ARENLLTLGQ WELVLPWIVP MPLALEINQR LLIMGLFSLD R SYEEVKAA ...String:
MAAMEANIFC TFDHKLSIAD VGKLTKLVAA VVPIPQRLHL IKHYQLGLHQ FVDHTRGYVR LRGLLRNMTL TLMRRVEGNQ ILLHVPTHG LLYTVLNTGP VTWEKGDALC VLPPLFHGPL ARENLLTLGQ WELVLPWIVP MPLALEINQR LLIMGLFSLD R SYEEVKAA VQQLQTITFR DATFTIPDPV IDQHLLIDMK TACLSMSMVA NLASELTMTY VRKLALEDSS MLLVKCQELL MR LDRERSV GEPRTPARPQ HVSPDDEIAR LSALFVMLRQ LDDLIREQVV FTVCDVSPDN KSATCIFKG

UniProtKB: Triplex capsid protein 2

-
Macromolecule #8: Large structural phosphoprotein

MacromoleculeName: Large structural phosphoprotein / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human herpesvirus 5 strain AD169
Molecular weightTheoretical: 112.829102 KDa
SequenceString: MSLQFIGLQR RDVVALVNFL RHLTQKPDVD LEAHPKILKK CGEKRLHRRT VLFNELMLWL GYYRELRFHN PDLSSVLEEF EVRCVAVAR RGYTYPFGDR GKARDHLAVL DRTEFDTDVR HDAEIVERAL VSAVILAKMS VRETLVTAIG QTEPIAFVHL K DTEVQRIE ...String:
MSLQFIGLQR RDVVALVNFL RHLTQKPDVD LEAHPKILKK CGEKRLHRRT VLFNELMLWL GYYRELRFHN PDLSSVLEEF EVRCVAVAR RGYTYPFGDR GKARDHLAVL DRTEFDTDVR HDAEIVERAL VSAVILAKMS VRETLVTAIG QTEPIAFVHL K DTEVQRIE ENLEGVRRNM FCVKPLDLNL DRHANTALVN AVNKLVYTGR LIMNVRRSWE ELERKCLARI QERCKLLVKE LR MCLSFDS NYCRNILKHA VENGDSADTL LELLIEDFDI YVDSFPQSAH TFLGARSPSL EFDDDANLLS LGGGSAFSSV PKK HVPTQP LDGWSWIASP WKGHKPFRFE AHGSLAPAAE AHAARSAAVG YYDEEEKRRE RQKRVDDEVV QREKQQLKAW EERQ QNLQQ RQQQPPPPAR KPSASRRLFG SSADEDDDDD DDEKNIFTPI KKPGTSGKGA ASGGGVSSIF SGLLSSGSQK PTSGP LNIP QQQQRHAAFS LVSPQVTKAS PGRVRRDSAW DVRPLTETRG DLFSGDEDSD SSDGYPPNRQ DPRFTDTLVD ITDTET SAK PPVTTAYKFE QPTLTFGAGV NVPAGAGAAI LTPTPVNPST APAPAPTPTF AGTQTPVNGN SPWAPTAPLP GDMNPAN WP RERAWALKNP HLAYNPFRMP TTSTASQNTV STTPRRPSTP RAAVTQTASR DAADEVWALR DQTAESPVED SEEEDDDS S DTGSVVSLGH TTPSSDYNND VISPPSQTPE QSTPSRIRKA KLSSPMTTTS TSQKPVLGKR VATPHASARA QTVTSTPVQ GRLEKQVSGT PSTVPATLLQ PQPASSKTTS SRNVTSGAGT SSASSARQPS ASASVLSPTE DDVVSPATSP LSMLSSASPS PAKSAPPSP VKGRGSRVGV PSLKPTLGGK AVVGRPPSVP VSGSAPGRLS GSSRAASTTP TYPAVTTVYP PSSTAKSSVS N APPVASPS ILKPGASAAL QSRRSTGTAA VGSPVKSTTG MKTVAFDLSS PQKSGTGPQP GSAGMGGAKT PSDAVQNILQ KI EKIKNTE E

UniProtKB: Large structural phosphoprotein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 8.0 sec. / Average electron dose: 47.2 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Particle selectionNumber selected: 367007
Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final reconstructionApplied symmetry - Point group: C5 (5 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.27 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 69628
FSC plot (resolution estimation)

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more