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- EMDB-40660: Cryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the pr... -

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Basic information

Entry
Database: EMDB / ID: EMD-40660
TitleCryo-EM structure of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
Map dataSharpened full map of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
Sample
  • Complex: ssDNA-bound human CST-POT1(ESDL)/TPP1 complex
    • Protein or peptide: CST complex subunit CTC1
    • Protein or peptide: CST complex subunit STN1
    • Protein or peptide: CST complex subunit TEN1
    • Protein or peptide: Protection of telomeres protein 1
    • Protein or peptide: TPP1
    • DNA: DNA (5'-D(*TP*TP*AP*GP*GP*GP*TP*TP*AP*G)-3')
  • Ligand: ZINC ION
Keywordstelomere / shelterin / cst / complex / DNA BINDING PROTEIN
Function / homology
Function and homology information


positive regulation of DNA strand elongation / positive regulation of telomeric D-loop disassembly / G-rich single-stranded DNA binding / CST complex / telomere assembly / segmentation / urogenital system development / 8-hydroxy-2'-deoxyguanosine DNA binding / telomeric D-loop binding / regulation of double-strand break repair via nonhomologous end joining ...positive regulation of DNA strand elongation / positive regulation of telomeric D-loop disassembly / G-rich single-stranded DNA binding / CST complex / telomere assembly / segmentation / urogenital system development / 8-hydroxy-2'-deoxyguanosine DNA binding / telomeric D-loop binding / regulation of double-strand break repair via nonhomologous end joining / protection from non-homologous end joining at telomere / DEAD/H-box RNA helicase binding / telomerase inhibitor activity / establishment of protein localization to telomere / regulation of establishment of protein localization to telomere / telomeric D-loop disassembly / telomere maintenance via telomere lengthening / shelterin complex / Telomere C-strand synthesis initiation / regulation of telomere maintenance via telomerase / Telomere C-strand (Lagging Strand) Synthesis / nuclear telomere cap complex / single-stranded telomeric DNA binding / G-rich strand telomeric DNA binding / telomere capping / intermediate filament cytoskeleton / Processive synthesis on the C-strand of the telomere / Polymerase switching on the C-strand of the telomere / telomerase holoenzyme complex / Removal of the Flap Intermediate from the C-strand / bone marrow development / embryonic limb morphogenesis / protein localization to chromosome, telomeric region / telomeric DNA binding / hematopoietic stem cell proliferation / negative regulation of telomere maintenance via telomerase / positive regulation of telomere maintenance / replicative senescence / Telomere Extension By Telomerase / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / telomere maintenance via telomerase / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / spleen development / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / regulation of G2/M transition of mitotic cell cycle / Packaging Of Telomere Ends / DNA polymerase binding / positive regulation of telomere maintenance via telomerase / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / telomere maintenance / Inhibition of DNA recombination at telomere / Meiotic synapsis / bioluminescence / thymus development / positive regulation of DNA replication / skeletal system development / picornain 2A / generation of precursor metabolites and energy / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / intracellular protein transport / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / DNA Damage/Telomere Stress Induced Senescence / multicellular organism growth / fibrillar center / positive regulation of fibroblast proliferation / single-stranded DNA binding / nucleoside-triphosphate phosphatase / outer membrane-bounded periplasmic space / channel activity / monoatomic ion transmembrane transport / chromosome, telomeric region / DNA replication / RNA helicase activity / nuclear body / endocytosis involved in viral entry into host cell / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / intracellular membrane-bounded organelle / DNA-templated transcription / DNA damage response / protein-containing complex binding / virion attachment to host cell / host cell nucleus / structural molecule activity / ATP hydrolysis activity / proteolysis / RNA binding / zinc ion binding
Similarity search - Function
CST complex subunit Ten1, animal and plant type / CST complex subunit CTC1 / CST complex subunit CTC1-like / CST, telomere maintenance, complex subunit CTC1 / Telomere-capping, CST complex subunit / CST complex subunit Stn1 / Stn1, C-terminal / CST complex subunit Stn1, wHTH1 motif superfamily / CST, complex subunit STN1, C terminal / : ...CST complex subunit Ten1, animal and plant type / CST complex subunit CTC1 / CST complex subunit CTC1-like / CST, telomere maintenance, complex subunit CTC1 / Telomere-capping, CST complex subunit / CST complex subunit Stn1 / Stn1, C-terminal / CST complex subunit Stn1, wHTH1 motif superfamily / CST, complex subunit STN1, C terminal / : / Protection of telomeres protein 1 (POT1), C-terminal insertion domain / Protection of telomeres protein 1, ssDNA-binding domain / ssDNA-binding domain of telomere protection protein / Adrenocortical dysplasia protein / Shelterin complex subunit TPP1/Est3 / Shelterin complex subunit, TPP1/ACD / Replication factor A protein-like / Protection of telomeres protein 1 / Telomeric single stranded DNA binding POT1/Cdc13 / Telomeric single stranded DNA binding POT1/CDC13 / Telomeric single stranded DNA binding POT1/CDC13 / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid binding domain / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Picornavirus coat protein / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / Winged helix DNA-binding domain superfamily / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Reverse transcriptase/Diguanylate cyclase domain / Winged helix-like DNA-binding domain superfamily / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Nucleic acid-binding, OB-fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Genome polyprotein / Maltose/maltodextrin-binding periplasmic protein / CST complex subunit CTC1 / CST complex subunit TEN1 / Adrenocortical dysplasia protein homolog / CST complex subunit STN1 / Protection of telomeres protein 1
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.1 Å
AuthorsCai SW
Funding support United States, 2 items
OrganizationGrant numberCountry
Other privateBCRF-22-036
National Institutes of Health/National Cancer Institute (NIH/NCI)R35 CA210036 United States
CitationJournal: bioRxiv / Year: 2023
Title: POT1 recruits and regulates CST-Polα/Primase at human telomeres.
Authors: Sarah W Cai / Hiroyuki Takai / Thomas Walz / Titia de Lange /
Abstract: Telomere maintenance requires extension of the G-rich telomeric repeat strand by telomerase and fill-in synthesis of the C-rich strand by Polα/Primase. Telomeric Polα/Primase is bound to Ctc1-Stn1- ...Telomere maintenance requires extension of the G-rich telomeric repeat strand by telomerase and fill-in synthesis of the C-rich strand by Polα/Primase. Telomeric Polα/Primase is bound to Ctc1-Stn1-Ten1 (CST), a single-stranded DNA-binding complex. Like mutations in telomerase, mutations affecting CST-Polα/Primase result in pathological telomere shortening and cause a telomere biology disorder, Coats plus (CP). We determined cryogenic electron microscopy structures of human CST bound to the shelterin heterodimer POT1/TPP1 that reveal how CST is recruited to telomeres by POT1. Phosphorylation of POT1 is required for CST recruitment, and the complex is formed through conserved interactions involving several residues mutated in CP. Our structural and biochemical data suggest that phosphorylated POT1 holds CST-Polα/Primase in an inactive auto-inhibited state until telomerase has extended the telomere ends. We propose that dephosphorylation of POT1 releases CST-Polα/Primase into an active state that completes telomere replication through fill-in synthesis.
History
DepositionApr 28, 2023-
Header (metadata) releaseJun 7, 2023-
Map releaseJun 7, 2023-
UpdateOct 16, 2024-
Current statusOct 16, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40660.png

Downloads & links

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Map

FileDownload / File: emd_40660.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSharpened full map of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.86 Å/pix.
x 352 pix.
= 302.72 Å		0.86 Å/pix.
x 352 pix.
= 302.72 Å		0.86 Å/pix.
x 352 pix.
= 302.72 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.86 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.15
Minimum - Maximum-0.9851709 - 1.736532
Average (Standard dev.)0.0020478792 (±0.03273432)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions352352352
Spacing352352352
CellA=B=C: 302.72 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_40660_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B of human CST bound to...

Fileemd_40660_half_map_1.map
AnnotationHalf map B of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A of human CST bound to...

Fileemd_40660_half_map_2.map
AnnotationHalf map A of human CST bound to POT1(ESDL)/TPP1 in the presence of telomeric ssDNA
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : ssDNA-bound human CST-POT1(ESDL)/TPP1 complex

EntireName: ssDNA-bound human CST-POT1(ESDL)/TPP1 complex
Components
  • Complex: ssDNA-bound human CST-POT1(ESDL)/TPP1 complex
    • Protein or peptide: CST complex subunit CTC1
    • Protein or peptide: CST complex subunit STN1
    • Protein or peptide: CST complex subunit TEN1
    • Protein or peptide: Protection of telomeres protein 1
    • Protein or peptide: TPP1
    • DNA: DNA (5'-D(*TP*TP*AP*GP*GP*GP*TP*TP*AP*G)-3')
  • Ligand: ZINC ION

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Supramolecule #1: ssDNA-bound human CST-POT1(ESDL)/TPP1 complex

SupramoleculeName: ssDNA-bound human CST-POT1(ESDL)/TPP1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6 / Details: CST-POT1(ESDL)/TPP1 complex in the presence of DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 370 KDa

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Macromolecule #1: CST complex subunit CTC1

MacromoleculeName: CST complex subunit CTC1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 178.300609 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MGSSHHHHHH SSGTKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGL LAEITPDKAF QDKLYPFTWD AVRYNGKLIA YPIAVEALSL IYNKDLLPNP PKTWEEIPAL DKELKAKGKS A LMFNLQEP ...String:
MGSSHHHHHH SSGTKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGL LAEITPDKAF QDKLYPFTWD AVRYNGKLIA YPIAVEALSL IYNKDLLPNP PKTWEEIPAL DKELKAKGKS A LMFNLQEP YFTWPLIAAD GGYAFKYENG KYDIKDVGVD NAGAKAGLTF LVDLIKNKHM NADTDYSIAE AAFNKGETAM TI NGPWAWS NIDTSKVNYG VTVLPTFKGQ PSKPFVGVLS AGINAASPNK ELAKEFLENY LLTDEGLEAV NKDKPLGAVA LKS YEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTKLVEKY LEVLFQGPGS MAAG RAQVP SSEQAWLEDA QVFIQKTLCP AVKEPNVQLT PLVIDCVKTV WLSQGRNQGS TLPLSYSFVS VQDLKTHQRL PCCSH LSWS SSAYQAWAQE AGPNGNPLPR EQLLLLGTLT DLSADLEQEC RNGSLYVRDN TGVLSCELID LDLSWLGHLF LFPRWS YLP PARWNSSGEG HLELWDAPVP VFPLTISPGP VTPIPVLYPE SASCLLRLRN KLRGVQRNLA GSLVRLSALV KSKQKAY FI LSLGRSHPAV THVSIIVQVP AQLVWHRALR PGTAYVLTEL RVSKIRGQRQ HVWMTSQSSR LLLLKPECVQ ELELELEG P LLEADPKPLP MPSNSEDKKD PESLVRYSRL LSYSGAVTGV LNEPAGLYEL DGQLGLCLAY QQFRGLRRVM RPGVCLQLQ DVHLLQSVGG GTRRPVLAPC LRGAVLLQSF SRQKPGAHSS RQAYGASLYE QLVWERQLGL PLYLWATKAL EELACKLCPH VLRHHQFLQ HSSPGSPSLG LQLLAPTLDL LAPPGSPVRN AHNEILEEPH HCPLQKYTRL QTPSSFPTLA TLKEEGQRKA W ASFDPKAL LPLPEASYLP SCQLNRRLAW SWLCLLPSAF CPAQVLLGVL VASSHKGCLQ LRDQSGSLPC LLLAKHSQPL SD PRLIGCL VRAERFQLIV ERDVRSSFPS WKELSMPGFI QKQQARVYVQ FFLADALILP VPRPCLHSAT PSTPQTDPTG PEG PHLGQS RLFLLCHKEA LMKRNFCVPP GASPEVPKPA LSFYVLGSWL GGTQRKEGTG WGLPEPQGND DNDQKVHLIF FGSS VRWFE FLHPGQVYRL IAPGPATPML FEKDGSSCIS RRPLELAGCA SCLTVQDNWT LELESSQDIQ DVLDANKSLP ESSLT DLLS DNFTDSLVSF SAEILSRTLC EPLVASLWMK LGNTGAMRRC VKLTVALETA ECEFPPHLDV YIEDPHLPPS LGLLPG ARV HFSQLEKRVS RSHNVYCCFR SSTYVQVLSF PPETTISIPL PHIYLAELLQ GGQSPFQATA SCHIVSVFSL QLFWVCA YC TSICRQGKCT RLGSTCPTQT AISQAIIRLL VEDGTAEAVV TCRNHHVAAA LGLCPREWAS LLDFVQVPGR VVLQFAGP G AQLESSARVD EPMTMFLWTL CTSPSVLRPI VLSFELERKP SKIVPLEPPR LQRFQCGELP FLTHVNPRLR LSCLSIRES EYSSSLGILA SSC

UniProtKB: Maltose/maltodextrin-binding periplasmic protein, CST complex subunit CTC1

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Macromolecule #2: CST complex subunit STN1

MacromoleculeName: CST complex subunit STN1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 42.172949 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MQPGSSRCEE ETPSLLWGLD PVFLAFAKLY IRDILDMKES RQVPGVFLYN GHPIKQVDVL GTVIGVRERD AFYSYGVDDS TGVINCICW KKLNTESVSA APSAARELSL TSQLKKLQET IEQKTKIEIG DTIRVRGSIR TYREEREIHA TTYYKVDDPV W NIQIARML ...String:
MQPGSSRCEE ETPSLLWGLD PVFLAFAKLY IRDILDMKES RQVPGVFLYN GHPIKQVDVL GTVIGVRERD AFYSYGVDDS TGVINCICW KKLNTESVSA APSAARELSL TSQLKKLQET IEQKTKIEIG DTIRVRGSIR TYREEREIHA TTYYKVDDPV W NIQIARML ELPTIYRKVY DQPFHSSALE KEEALSNPGA LDLPSLTSLL SEKAKEFLME NRVQSFYQQE LEMVESLLSL AN QPVIHSA SSDQVNFKKD TTSKAIHSIF KNAIQLLQEK GLVFQKDDGF DNLYYVTRED KDLHRKIHRI IQQDCQKPNH MEK GCHFLH ILACARLSIR PGLSEAVLQQ VLELLEDQSD IVSTMEHYYT AF

UniProtKB: CST complex subunit STN1

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Macromolecule #3: CST complex subunit TEN1

MacromoleculeName: CST complex subunit TEN1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.872013 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MMLPKPGTYY LPWEVSAGQV PDGSTLRTFG RLCLYDMIQS RVTLMAQHGS DQHQVLVCTK LVEPFHAQVG SLYIVLGELQ HQQDRGSVV KARVLTCVEG MNLPLLEQAI REQRLYKQER GGSQ

UniProtKB: CST complex subunit TEN1

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Macromolecule #4: Protection of telomeres protein 1

MacromoleculeName: Protection of telomeres protein 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.938219 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHHHHHHGSS LVPATNYIYT PLNQLKGGTI VNVYGVVKFF KPPYLSKGTD YCSVVTIVDQ TNVKLTCLLF SGNYEALPII YKNGDIVRF HRLKIQVYKK ETQGITSSGF ASLTFEGTLG APIIPRTSSK YFNFTTEDHK MVEALRVWAS THMSPSWTLL K LCDVQPMQ ...String:
MHHHHHHGSS LVPATNYIYT PLNQLKGGTI VNVYGVVKFF KPPYLSKGTD YCSVVTIVDQ TNVKLTCLLF SGNYEALPII YKNGDIVRF HRLKIQVYKK ETQGITSSGF ASLTFEGTLG APIIPRTSSK YFNFTTEDHK MVEALRVWAS THMSPSWTLL K LCDVQPMQ YFDLTCQLLG KAEVDGASFL LKVWDGTRTP FPSWRVLIQD LVLEGDLSHI HRLQNLTIDI LVYDNHVHVA RS LKVGSFL RIYSLHTKLQ SMNSENQTML SLEFHLHGGT SYGRGIRVLP ESNSDVDQLK KDLESANLTA NQHSDVICQS EPD DSFPSS GSESDLVSLY EVERCQQLSA TILTDHQYLE RTPLCAILKQ KAPQQYRIRA KLRSYKPRRL FQSVKLHCPK CHLL QEVPH EGDLDIIFQD GATKTPDVKL QNTSLYDSKI WTTKNQKGRK VAVHFVKNNG ILPLSNECLL LIEGGTLSEI CKLSN KFNS VIPVRSGHED LELLDLSAPF LIQGTIHHYG CKQCSSLRSI QNLNSLVDKT SWIPSSVAEA LGIVPLQYVF VMTFTL DDG TGVLEAYLMD SDKFFQIPAS EVLMDDDLQK SVDMIMDMFC PPGIKIDAYP WLECFIKSYN VTNGTDNQIC YQIFDTT VA EDVI

UniProtKB: Protection of telomeres protein 1

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Macromolecule #5: TPP1

MacromoleculeName: TPP1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: picornain 2A
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.064863 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG SVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWP TLVTTLTYGV QCFSRYPDHM KQHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI D FKEDGNIL ...String:
MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG SVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWP TLVTTLTYGV QCFSRYPDHM KQHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI D FKEDGNIL GHKLEYNYNS HNVYIMADKQ KNGIKVNFKI RHNIEDGSVQ LADHYQQNTP IGDGPVLLPD NHYLSTQSAL SK DPNEKRD HMVLLEFVTA AGITLGMDEL YKENLYFQGG SMAGSGRLVL RPWIRELILG SETPSSPRAG QLLEVLQDAE AAV AGPSHA PDTSDVGATL LVSDGTHSVR CLVTREALDT SDWEEKEFGF RGTEGRLLLL QDCGVHVQVA EGGAPAEFYL QVDR FSLLP TEQPRLRVPG CNQDLDVQKK LYDCLEEHLS ESTSSNAGLS LSQLLDEMRE DQEHQGALVC LAESCLTLEG PCTAP PVTH WAASRCKATG EAVYTVPSSM LCISENDQLI LSSLGPCQRT QGPEL

UniProtKB: Genome polyprotein, Adrenocortical dysplasia protein homolog

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Macromolecule #6: DNA (5'-D(*TP*TP*AP*GP*GP*GP*TP*TP*AP*G)-3')

MacromoleculeName: DNA (5'-D(*TP*TP*AP*GP*GP*GP*TP*TP*AP*G)-3') / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 5.682672 KDa
SequenceString:
(DG)(DG)(DT)(DT)(DA)(DG)(DG)(DG)(DT)(DT) (DA)(DG)(DG)(DG)(DT)(DT)(DA)(DG)

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Macromolecule #7: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 7 / Number of copies: 2 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.02 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.3 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 76359
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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