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- EMDB-19132: Structure of dynein-2 intermediate chain DYNC2I2 (WDR34) in compl... -
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Open data
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Basic information
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Title | Structure of dynein-2 intermediate chain DYNC2I2 (WDR34) in complex with dynein-2 heavy chain DYNC2H1. | ||||||||||||||||||||||||||||||
![]() | Locally refined map, locally sharpened with locscale | ||||||||||||||||||||||||||||||
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![]() | dynein / cilia / intraflagellar transport / complex / TRANSPORT PROTEIN | ||||||||||||||||||||||||||||||
Function / homology | ![]() MGMT-mediated DNA damage reversal / nitric-oxide synthase inhibitor activity / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / visual behavior / intraciliary retrograde transport / methylated-DNA-[protein]-cysteine S-methyltransferase / methylated-DNA-[protein]-cysteine S-methyltransferase activity / cilium movement involved in cell motility / 9+2 motile cilium ...MGMT-mediated DNA damage reversal / nitric-oxide synthase inhibitor activity / deoxyribonuclease inhibitor activity / negative regulation of DNA strand resection involved in replication fork processing / visual behavior / intraciliary retrograde transport / methylated-DNA-[protein]-cysteine S-methyltransferase / methylated-DNA-[protein]-cysteine S-methyltransferase activity / cilium movement involved in cell motility / 9+2 motile cilium / intraciliary transport / dynein light chain binding / spinal cord motor neuron differentiation / motile cilium assembly / dynein heavy chain binding / DNA-methyltransferase activity / Activation of BIM and translocation to mitochondria / embryonic skeletal system morphogenesis / ciliary tip / Intraflagellar transport / negative regulation of nitric oxide biosynthetic process / dynein complex / DNA ligation / negative regulation of phosphorylation / COPI-independent Golgi-to-ER retrograde traffic / coronary vasculature development / minus-end-directed microtubule motor activity / non-motile cilium assembly / DNA alkylation repair / dynein light intermediate chain binding / protein localization to cilium / cytoplasmic dynein complex / positive regulation of smoothened signaling pathway / ciliary plasm / dorsal/ventral pattern formation / enzyme inhibitor activity / determination of left/right symmetry / embryonic limb morphogenesis / positive regulation of double-strand break repair / microtubule motor activity / ciliary base / dynein intermediate chain binding / Macroautophagy / pericentriolar material / microtubule-based movement / Golgi organization / cytoskeletal motor activity / axoneme / positive regulation of insulin secretion involved in cellular response to glucose stimulus / tertiary granule membrane / ficolin-1-rich granule membrane / spermatid development / cilium assembly / Hedgehog 'off' state / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / forebrain development / Recruitment of mitotic centrosome proteins and complexes / axon cytoplasm / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / Resolution of Sister Chromatid Cohesion / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / substantia nigra development / MHC class II antigen presentation / centriole / AURKA Activation by TPX2 / ciliary basal body / filopodium / kidney development / methyltransferase activity / RHO GTPases Activate Formins / HCMV Early Events / cilium / protein processing / mitotic spindle / kinetochore / Aggrephagy / Separation of Sister Chromatids / Regulation of PLK1 Activity at G2/M Transition / apical part of cell / site of double-strand break / scaffold protein binding / methylation / microtubule / cytoskeleton / DNA repair / centrosome / DNA damage response / Neutrophil degranulation / negative regulation of apoptotic process / protein-containing complex binding / apoptotic process / enzyme binding / Golgi apparatus / ATP hydrolysis activity Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.0 Å | ||||||||||||||||||||||||||||||
![]() | Mukhopadhyay AG / Toropova K / Daly L / Wells J / Vuolo L / Mladenov M / Seda M / Jenkins D / Stephens DJ / Roberts AJ | ||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and tethering mechanism of dynein-2 intermediate chains in intraflagellar transport. Authors: Aakash G Mukhopadhyay / Katerina Toropova / Lydia Daly / Jennifer N Wells / Laura Vuolo / Miroslav Mladenov / Marian Seda / Dagan Jenkins / David J Stephens / Anthony J Roberts / ![]() Abstract: Dynein-2 is a large multiprotein complex that powers retrograde intraflagellar transport (IFT) of cargoes within cilia/flagella, but the molecular mechanism underlying this function is still emerging. ...Dynein-2 is a large multiprotein complex that powers retrograde intraflagellar transport (IFT) of cargoes within cilia/flagella, but the molecular mechanism underlying this function is still emerging. Distinctively, dynein-2 contains two identical force-generating heavy chains that interact with two different intermediate chains (WDR34 and WDR60). Here, we dissect regulation of dynein-2 function by WDR34 and WDR60 using an integrative approach including cryo-electron microscopy and CRISPR/Cas9-enabled cell biology. A 3.9 Å resolution structure shows how WDR34 and WDR60 use surprisingly different interactions to engage equivalent sites of the two heavy chains. We show that cilia can assemble in the absence of either WDR34 or WDR60 individually, but not both subunits. Dynein-2-dependent distribution of cargoes depends more strongly on WDR60, because the unique N-terminal extension of WDR60 facilitates dynein-2 targeting to cilia. Strikingly, this N-terminal extension can be transplanted onto WDR34 and retain function, suggesting it acts as a flexible tether to the IFT "trains" that assemble at the ciliary base. We discuss how use of unstructured tethers represents an emerging theme in IFT train interactions. | ||||||||||||||||||||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 3.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 32.9 KB 32.9 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 19.2 KB | Display | ![]() |
Images | ![]() | 112 KB | ||
Masks | ![]() | 103 MB | ![]() | |
Filedesc metadata | ![]() | 10.3 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() | 95.6 MB 95.6 MB 4.8 MB 95.7 MB 95.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 21.9 KB | Display | |
Data in CIF | ![]() | 29.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8rggMC ![]() 8rghC ![]() 8rgiC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Locally refined map, locally sharpened with locscale | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.828 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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-Additional map: Locally refined map, unsharpened
File | emd_19132_additional_1.map | ||||||||||||
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Annotation | Locally refined map, unsharpened | ||||||||||||
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-Additional map: Globally refined map, unsharpened
File | emd_19132_additional_2.map | ||||||||||||
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Annotation | Globally refined map, unsharpened | ||||||||||||
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-Additional map: Composite map of locally refined WDR34 and WDR60 map regions.
File | emd_19132_additional_3.map | ||||||||||||
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Annotation | Composite map of locally refined WDR34 and WDR60 map regions. | ||||||||||||
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-Half map: #2
File | emd_19132_half_map_1.map | ||||||||||||
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-Half map: #1
File | emd_19132_half_map_2.map | ||||||||||||
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Sample components
-Entire : Dynein-2 complex
Entire | Name: Dynein-2 complex |
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Components |
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-Supramolecule #1: Dynein-2 complex
Supramolecule | Name: Dynein-2 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Methylated-DNA--protein-cysteine methyltransferase,Cytoplasmic dy...
Macromolecule | Name: Methylated-DNA--protein-cysteine methyltransferase,Cytoplasmic dynein 2 heavy chain 1 type: protein_or_peptide / ID: 1 / Details: DYNC2H1 with N-terminal SNAPf tag / Number of copies: 1 / Enantiomer: LEVO EC number: methylated-DNA-[protein]-cysteine S-methyltransferase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 515.223031 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GDKDCEMKRT TLDSPLGKLE LSGCEQGLHR IIFLGKGTSA ADAVEVPAPA AVLGGPEPLM QATAWLNAYF HQPEAIEEFP VPALHHPVF QQESFTRQVL WKLLKVVKFG EVISYSHLAA LAGNPAATAA VKTALSGNPV PILIPCHRVV QGDLDVGGYE G GLAVKEWL ...String: GDKDCEMKRT TLDSPLGKLE LSGCEQGLHR IIFLGKGTSA ADAVEVPAPA AVLGGPEPLM QATAWLNAYF HQPEAIEEFP VPALHHPVF QQESFTRQVL WKLLKVVKFG EVISYSHLAA LAGNPAATAA VKTALSGNPV PILIPCHRVV QGDLDVGGYE G GLAVKEWL LAHEGHRLGK PGLGGSLEVL FQGPDYDIPT TLEVLFQGPA NGTADVRKLF IFTTTQNYFG LMSELWDQPL LC NCLEINN FLDDGNQMLL RVQRSDAGIS FSNTIEFGDT KDKVLVFFKL RPEVITDENL HDNILVSSML ESPISSLYQA VRQ VFAPML LKDQEWSRNF DPKLQNLLSE LEAGLGIVLR RSDTNLTKLK FKEDDTRGIL TPSDEFQFWI EQAHRGNKQI SKER ANYFK ELFETIAREF YNLDSLSLLE VVDLVETTQD VVDDVWRQTE HDHYPESRML HLLDIIGGSF GRFVQKKLGT LNLWE DPYY LVKESLKAGI SICEQWVIVC NHLTGQVWQR YVPHPWKNEK YFPETLDKLG KRLEEVLAIR TIHEKFLYFL PASEEK IIC LTRVFEPFTG LNPVQYNPYT EPLWKAAVSQ YEKIIAPAEQ KIAGKLKNYI SEIQDSPQQL LQAFLKYKEL VKRPTIS KE LMLERETLLA RLVDSIKDFR LDFENRCRGI PGDASGPLSG KNLSEVVNSI VWVRQLELKV DDTIKIAEAL LSDLPGFR C FHQSAKDLLD QLKLYEQEQF DDWSRDIQSG LSDSRSGLCI EASSRIMELD SNDGLLKVHY SDRLVILLRE VRQLSALGF VIPAKIQQVA NIAQKFCKQA IILKQVAHFY NSIDQQMIQS QRPMMLQSAL AFEQIIKNSK AGSGGKSQIT WDNPKELEGY IQKLQNAAE RLATENRKLR KWHTTFCEKV VVLMNIDLLR QQQRWKDGLQ ELRTGLATVE AQGFQASDMH AWKQHWNHQL Y KALEHQYQ MGLEALNENL PEINIDLTYK QGRLQFRPPF EEIRAKYYRE MKRFIGIPNQ FKGVGEAGDE SIFSIMIDRN AS GFLTIFS KAEDLFRRLS AVLHQHKEWI VIGQVDMEAL VEKHLFTVHD WEKNFKALKI KGKEVERLPS AVKVDCLNIN CNP VKTVID DLIQKLFDLL VLSLKKSIQA HLHEIDTFVT EAMEVLTIMP QSVEEIGDAN LQYSKLQERK PEILPLFQEA EDKN RLLRT VAGGGLETIS NLKAKWDKFE LMMESHQLMI KDQIEVMKGN VKSRLQIYYQ ELEKFKARWD QLKPGDDVIE TGQHN TLDK SAKLIKEKKI EFDDLEVTRK KLVDDCHHFR LEEPNFSLAS SISKDIESCA QIWAFYEEFQ QGFQEMANED WITFRT KTY LFEEFLMNWH DRLRKVEEHS VMTVKLQSEV DKYKIVIPIL KYVRGEHLSP DHWLDLFRLL GLPRGTSLEK LLFGDLL RV ADTIVAKAAD LKDLNSRAQG EVTIREALRE LDLWGVGAVF TLIDYEDSQS RTMKLIKDWK DIVNQVGDNR CLLQSLKD S PYYKGFEDKV SIWERKLAEL DEYLQNLNHI QRKWVYLEPI FGRGALPKEQ TRFNRVDEDF RSIMTDIKKD NRVTTLTTH AGIRNSLLTI LDQLQRCQRS LNEFLEEKRS AFPRFYFIGD DDLLEILGQS TNPSVIQSHL KKLFAGINSV CFDEKSKHIT AMKSLEGEV VPFKNKVPLS NNVETWLNDL ALEMKKTLEQ LLKECVTTGR SSQGAVDPSL FPSQILCLAE QIKFTEDVEN A IKDHSLHQ IETQLVNKLE QYTNIDTSSE DPGNTESGIL ELKLKALILD IIHNIDVVKQ LNQIQVHTTE DWAWKKQLRF YM KSDHTCC VQMVDSEFQY TYEYQGNASK LVYTPLTDKC YLTLTQAMKM GLGGNPYGPA GTGKTESVKA LGGLLGRQVL VFN CDEGID VKSMGRIFVG LVKCGAWGCF DEFNRLEESV LSAVSMQIQT IQDALKNHRT VCELLGKEVE VNSNSGIFIT MNPA GKGYG GRQKLPDNLK QLFRPVAMSH PDNELIAEVI LYSEGFKDAK VLSRKLVAIF NLSRELLTPQ QHYDWGLRAL KTVLR GSGN LLRQLNKSGT TQNANESHIV VQALRLNTMS KFTFTDCTRF DALIKDVFPG IELKEVEYDE LSAALKQVFE EANYEI IPN QIKKALELYE QLCQRMGVVI VGPSGAGKST LWRMLRAALC KTGKVVKQYT MNPKAMPRYQ LLGHIDMDTR EWSDGVL TN SARQVVREPQ DVSSWIICDG DIDPEWIESL NSVLDDNRLL TMPSGERIQF GPNVNFVFET HDLSCASPAT ISRMGMIF L SDEETDLNSL IKSWLRNQPA EYRNNLENWI GDYFEKALQW VLKQNDYVVE TSLVGTVMNG LSHLHGCRDH DEFIINLIR GLGGNLNMKS RLEFTKEVFH WARESPPDFH KPMDTYYDST RGRLATYVLK KPEDLTADDF SNGLTLPVIQ TPDMQRGLDY FKPWLSSDT KQPFILVGPE GCGKGMLLRY AFSQLRSTQI ATVHCSAQTT SRHLLQKLSQ TCMVISTNTG RVYRPKDCER L VLYLKDIN LPKLDKWGTS TLVAFLQQVL TYQGFYDENL EWVGLENIQI VASMSAGGRL GRHKLTTRFT SIVRLCSIDY PE REQLQTI YGAYLEPVLH KNLKNHSIWG SSSKIYLLAG SMVQVYEQVR AKFTVDDYSH YFFTPCILTQ WVLGLFRYDL EGG SSNHPL DYVLEIVAYE ARRLFRDKIV GAKELHLFDI ILTSVFQGDW GSDILDNMSD SFYVTWGARH NSGARAAPGQ PLPP HGKPL GKLNSTDLKD VIKKGLIHYG RDNQNLDILL FHEVLEYMSR IDRVLSFPGG SLLLAGRSGV GRRTITSLVS HMHGA VLFS PKISRGYELK QFKNDLKHVL QLAGIEAQQV VLLLEDYQFV HPTFLEMINS LLSSGEVPGL YTLEELEPLL LPLKDQ ASQ DGFFGPVFNY FTYRIQQNLH IVLIMDSANS NFMINCESNP ALHKKCQVLW MEGWSNSSMK KIPEMLFSET GGGEKYN DK KRKEEKKKNS VDPDFLKSFL LIHESCKAYG ATPSQYMTFL HVYSAISSSK KKELLKRQSH LQAGVSKLNE AKALVDEL N RKAGEQSVLL KTKQDEADAA LQMITVSMQD ASEQKTELER LKHRIAEEVV KIEERKNKID DELKEVQPLV NEAKLAVGN IKPESLSEIR SLRMPPDVIR DILEGVLRLM GIFDTSWVSM KSFLAKRGVR EDIATFDARN ISKEIRESVE ELLFKNKGSF DPKNAKRAS TAAAPLAAWV KANIQYSHVL ERIHPLETEQ AGLESNLKKT EDRKRKLEEL LNSVGQKVSE LKEKFQSRTS E AAKLEAEV SKAQETIKAA EVLINQLDRE HKRWNAQVVE ITEELATLPK RAQLAAAFIT YLSAAPESLR KTCLEEWTKS AG LEKFDLR RFLCTESEQL IWKSEGLPSD DLSIENALVI LQSRVCPFLI DPSSQATEWL KTHLKDSRLE VINQQDSNFI TAL ELAVRF GKTLIIQEMD GVEPVLYPLL RRDLVAQGPR YVVQIGDKII DYNEEFRLFL STRNPNPFIP PDAASIVTEV NFTT TRSGL RGQLLALTIQ HEKPDLEEQK TKLLQQEEDK KIQLAKLEES LLETLATSQG NILENKDLIE SLNQTKASSA LIQES LKES YKLQISLDQE RDAYLPLAES ASKMYFIISD LSKINNMYRF SLAAFLRLFQ RALQNKQDSE NTEQRIQSLI SSLQHM VYE YICRCLFKAD QLMFALHFVR GMHPELFQEN EWDTFTGVVV GDMLRKADSQ QKIRDQLPSW IDQERSWAVA TLKIALP SL YQTLCFEDAA LWRTYYNNSM CEQEFPSILA KKVSLFQQIL VVQVLRPDRL QSAMALFACK TLGLKEVSPL PLNLKRLY K ETLEIEPILI IISPGADPSQ ELQELANAER SGECYHQVAM GQGQADLAIQ MLKECARNGD WLCLKNLHLV VSWLPVLEK ELNTLQPKDT FRLWLTAEVH PNFTPILLQS SLKITYESPP GLKKNLMRTY ESWTPEQISK KDNTHRAHAL FSLAWFHAAC QERRNYIPQ GWTKFYEFSL SDLRAGYNII DRLFDGAKDV QWEFVHGLLE NAIYGGRIDN YFDLRVLQSY LKQFFNSSVI D VFNQRNKK SIFPYSVSLP QSCSILDYRA VIEKIPEDDK PSFFGLPANI ARSSQRMISS QVISQLRILG RSITAGSKFD RE IWSNELS PVLNLWKKLN QNSNLIHQKV PPPNDRQGSP ILSFIILEQF NAIRLVQSVH QSLAALSKVI RGTTLLSSEV QKL ASALLN QKCPLAWQSK WEGPEDPLQY LRGLVARALA IQNWVDKAEK QALLSETLDL SELFHPDTFL NALRQETARA VGRS VDSLK FVASWKGRLQ EAKLQIKISG LLLEGCSFDG NQLSENQLDS PSVSSVLPCF MGWIPQDACG PYSPDECISL PVYTS AERD RVVTNIDVPC GGNQDQWIQC GAALFLKNQ UniProtKB: Methylated-DNA--protein-cysteine methyltransferase, Cytoplasmic dynein 2 heavy chain 1 |
-Macromolecule #2: Cytoplasmic dynein 2 intermediate chain 1
Macromolecule | Name: Cytoplasmic dynein 2 intermediate chain 1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 122.865156 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MEPGKRRTKD DTWKADDLRK HLWAIQSGGS KEERKHREKK LRKESEMDLP EHKEPRCRDP DQDARSRDRV AEVHTAKESP RGERDRDRQ RERRRDAKDR EKEKLKEKHR EAEKSHSRGK DREKEKDRRA RKEELRQTVA HHNLLGQETR DRQLLERAER K GRSVSKVR ...String: MEPGKRRTKD DTWKADDLRK HLWAIQSGGS KEERKHREKK LRKESEMDLP EHKEPRCRDP DQDARSRDRV AEVHTAKESP RGERDRDRQ RERRRDAKDR EKEKLKEKHR EAEKSHSRGK DREKEKDRRA RKEELRQTVA HHNLLGQETR DRQLLERAER K GRSVSKVR SEEKDEDSER GDEDRERRYR ERKLQYGDSK DNPLKYWLYK EEGERRHRKP REPDRDKKHR EKSSTREKRE KY SKEKSNS FSDKGEERHK EKRHKEGFHF DDERHQSNVD RKEKSAKDEP RKREFQNGEH RNRGASSKRD GTSSQHAENL VRN HGKDKD SRRKHGHEEG SSVWWKLDQR PGGEETVEIE KEETDLENAR ADAYTASCED DFEDYEDDFE VCDGDDDESS NEPE SREKL EELPLAQKKE IQEIQRAINA ENERIGELSL KLFQKRGRTE FEKEPRTDTN SSPSRASVCG IFVDFASASH RQKSR TQAL KQKMRSTKLL RLIDLDFSFT FSLLDLPPVN EYDMYIRNFG KKNTKQAYVQ CNEDNVERDI QTEEIETREV WTQHPG EST VVSGGSEQRD TSDAVVMPKI DTPRLCSFLR AACQVMAVLL EEDRLAAEPS WNLRAQDRAL YFSDSSSQLN TSLPFLQ NR KVSSLHTSRV QRQMVVSVHD LPEKSFVPLL DSKYVLCVWD IWQPSGPQKV LICESQVTCC CLSPLKAFLL FAGTAHGS V VVWDLREDSR LHYSVTLSDG FWTFRTATFS TDGILTSVNH RSPLQAVEPI STSVHKKQSF VLSPFSTQEE MSGLSFHIA SLDESGVLNV WVVVELPKAD IAGSISDLGL MPGGRVKLVH SALIQLGDSL SHKGNEFWGT TQTLNVKFLP SDPNHFIIGT DMGLISHGT RQDLRVAPKL FKPQQHGIRP VKVNVIDFSP FGEPIFLAGC SDGSIRLHQL SSAFPLLQWD SSTDSHAVTG L QWSPTRPA VFLVQDDTSN IYIWDLLQSD LGPVAKQQVS PNRLVAMAAV GEPEKAGGSF LALVLARASG SIDIQHLKRR WA APEVDEC NRLRLLLQEA LWPEGKLHK UniProtKB: Cytoplasmic dynein 2 intermediate chain 1 |
-Macromolecule #3: Cytoplasmic dynein 2 intermediate chain 2
Macromolecule | Name: Cytoplasmic dynein 2 intermediate chain 2 / type: protein_or_peptide / ID: 3 Details: DYNC2I2 (also known as WDR34) with C-terminal Strep tag Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 60.639129 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MATRAQPGPL SQAGSAGVAA LATVGVASGP GPGRPGPLQD ETLGVASVPS QWRAVQGIRG ETKSCQTASI ATASASAQAR NHVDAQVQT EAPVPVSVQP PSQYDIPRLA AFLRRVEAMV IRELNKNWQS HAFDGFEVNW TEQQQMVSCL YTLGYPPAQA Q GLHVTSIS ...String: MATRAQPGPL SQAGSAGVAA LATVGVASGP GPGRPGPLQD ETLGVASVPS QWRAVQGIRG ETKSCQTASI ATASASAQAR NHVDAQVQT EAPVPVSVQP PSQYDIPRLA AFLRRVEAMV IRELNKNWQS HAFDGFEVNW TEQQQMVSCL YTLGYPPAQA Q GLHVTSIS WNSTGSVVAC AYGRLDHGDW STLKSFVCAW NLDRRDLRPQ QPSAVVEVPS AVLCLAFHPT QPSHVAGGLY SG EVLVWDL SRLEDPLLWR TGLTDDTHTD PVSQVVWLPE PGHSHRFQVL SVATDGKVLL WQGIGVGQLQ LTEGFALVMQ QLP RSTKLK KHPRGETEVG ATAVAFSSFD PRLFILGTEG GFPLKCSLAA GEAALTRMPS SVPLRAPAQF TFSPHGGPIY SVSC SPFHR NLFLSAGTDG HVHLYSMLQA PPLTSLQLSL KYLFAVRWSP VRPLVFAAAS GKGDVQLFDL QKSSQKPTVL IKQTQ DESP VYCLEFNSQQ TQLLAAGDAQ GTVKVWQLST EFTEQGPREA EDLDCLAAEV AAWSHPQFEK GSAGSAAGSG AGWSHP QFE K UniProtKB: Cytoplasmic dynein 2 intermediate chain 2 |
-Macromolecule #4: Dynein light chain roadblock-type 1
Macromolecule | Name: Dynein light chain roadblock-type 1 / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 10.934576 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI DPQNDLTFLR IRSKKNEIMV APDKDYFLI VIQNPTE UniProtKB: Dynein light chain roadblock-type 1 |
-Macromolecule #5: Dynein light chain 1, cytoplasmic
Macromolecule | Name: Dynein light chain 1, cytoplasmic / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 10.381899 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG UniProtKB: Dynein light chain 1, cytoplasmic |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |