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- EMDB-54211: Structure of the Ypt7 GEF complex Mon1-Ccz1 from Chaetomium Therm... -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Structure of the Ypt7 GEF complex Mon1-Ccz1 from Chaetomium Thermophilum | |||||||||
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![]() | longin domain / GEF / nucleotide exchange / endosome / autophagosome / CYTOSOLIC PROTEIN | |||||||||
Function / homology | ![]() Mon1-Ccz1 complex / protein targeting to vacuole / multivesicular body membrane / fungal-type vacuole membrane / vesicle-mediated transport / autophagy Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | |||||||||
![]() | Wilmes S / Schaefer J / Moeller A / Kuemmel D | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Mechanistic Adaptation of the Metazoan RabGEFs Mon1-Ccz1 and Fuzzy-Inturned Authors: Wilmes S / Toenjes J / Drechsler M / Ruf A / Schaefer J / Luerick A / Januliene D / Apelt S / Di Iorio D / Wegner SV / Loose M / Moeller A / Paululat A / Kuemmel D | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 160.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.5 KB 17.5 KB | Display Display | ![]() |
Images | ![]() | 42 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Others | ![]() ![]() | 302 MB 302 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 755 KB | Display | ![]() |
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Full document | ![]() | 754.5 KB | Display | |
Data in XML | ![]() | 16.5 KB | Display | |
Data in CIF | ![]() | 19.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9rs6MC ![]() 9rs7C ![]() 9rs8C ![]() 9rs9C 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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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.68 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_54211_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_54211_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Complex of the Rab7 GEF Mon1-Ccz1
Entire | Name: Complex of the Rab7 GEF Mon1-Ccz1 |
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Components |
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-Supramolecule #1: Complex of the Rab7 GEF Mon1-Ccz1
Supramolecule | Name: Complex of the Rab7 GEF Mon1-Ccz1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Vacuolar fusion protein MON1
Macromolecule | Name: Vacuolar fusion protein MON1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 72.198766 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GPLGSMTQNN APESVAAEGT VAGQQTDTTK PEPSSQPAPE PPSQVTTDFP PNNKPNDVPA TEPASSSPRP TEPPAPPPPK PTIALSPLD IATLTFPDGT RGTFPAPPQT SAQSVSTPSI ASGHVTPQRD TDTASITSVA GTLRGVTGTA GDLASLLAGD G LGRKSKAW ...String: GPLGSMTQNN APESVAAEGT VAGQQTDTTK PEPSSQPAPE PPSQVTTDFP PNNKPNDVPA TEPASSSPRP TEPPAPPPPK PTIALSPLD IATLTFPDGT RGTFPAPPQT SAQSVSTPSI ASGHVTPQRD TDTASITSVA GTLRGVTGTA GDLASLLAGD G LGRKSKAW RVLRAQQQAC GEGSGEEGEI TEIEGLGLGE GMEGFERELD NIPDTLPDDE RLALWKGKLK HYLILSSAGK PI WSRHGDL SLVNSTMGVV QTIISFYEGA RNPLLGFTAG KVRFVILIKG PLYFVAISRL RESDAQLRAQ LEALYMQILS TLT LPILTN IFAHRPSTDL RGPLQGTESL LASLADSFTK GSPSTLLSAL ECLRLRKSQR QAITNIFLKS RCEELLYGLL VAGG KLVSV IRPRKHSLHP SDLQLIFNML FESGGIKGNG GENWIPLCLP AFNNTGYLYM YVSFLDDKAP DDQNQPPESS NLDAS NKNS SNTPDDDLTA LILISPSREA FYALQSMRTR LVSQLLSTGY LSLIRSTALS GRPSITSILP KTPLLHFLYK SRPNVQ WCM SSLSSLTPPG ATATETLLAR RKLMSVYEEL HAALHARHAH LRVVYSTADE KEGEGLACLG WSTPAFEVYC VAPGCVG RA GMAREVNRVV QWARREEERL FILGGGVF UniProtKB: Vacuolar fusion protein MON1 |
-Macromolecule #2: CCZ1/INTU/HSP4 first Longin domain-containing protein
Macromolecule | Name: CCZ1/INTU/HSP4 first Longin domain-containing protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 75.867539 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: SMTTPVSPSP SGIIPAQLGF LAIYNPALGT TDETLEDQIV YYATASTLSQ ARRRHRRPRR RDRQRAQSVV KDSRPNAAGA TGDSEAVAE DKDPVSKEER HERLRQIGLA QGMVEFAKSF SDGEPVDTID TEKARVILVE VEEGWWILAS IDLTRLPLPQ I KTPTSSSA ...String: SMTTPVSPSP SGIIPAQLGF LAIYNPALGT TDETLEDQIV YYATASTLSQ ARRRHRRPRR RDRQRAQSVV KDSRPNAAGA TGDSEAVAE DKDPVSKEER HERLRQIGLA QGMVEFAKSF SDGEPVDTID TEKARVILVE VEEGWWILAS IDLTRLPLPQ I KTPTSSSA PPPAPNLNPL PPEPAYEYSS REVKPPSLLR ADLLRAYDLF LLHHGSSLSS LLASQGRAQL VASLTRFWDH FL ATWNVLL HGNPACDVFG GIKLAASGEL GIGVGEEERG SGEREVLEGL VERVEGLVDV VVGRYGGPPS EKGPEEEQWL GLG GEVGEE DGAVFLGVGA LDRKSLRGVV QWMEEVYVWG ENAFGKPRRD LSTGHFLLGL SECSEEELTS SQANPKAIFV ELKP SYQHP SRKIPPEDPQ PLGKVGPELP RDHTARLRPV IYVSQPFIYI LLFSEITPSP STWPTLAESL HAQLSPLQKP LLHST SYRP ERPVVETTSS SGTTTQHQIF DLVYDTETLT LQSTIPNIPD PFPYSATTPT GHSTGQQHHQ QSIWTRVEAL QTHAQI LAI LSSGRAIPTD PSSFTHLPWE EGERTCKTAR GWWIVWTRVV EHSPPDAVSL HHARDDDDND DDASCSVLGH LRSVSSS HA AGSTSSSSGS GFGLGAIPGL GGLGGWAADG ATRLAQGIGI DTRRYVEGLL TSLGR UniProtKB: CCZ1/INTU/HSP4 first Longin domain-containing protein, CCZ1/INTU/HSP4 first Longin domain-containing protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.8 mg/mL |
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Buffer | pH: 7.3 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS GLACIOS |
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Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |