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- EMDB-29338: Cryo-EM structure of Cryptococcus neoformans trehalose-6-phosphat... -
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Open data
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Basic information
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Title | Cryo-EM structure of Cryptococcus neoformans trehalose-6-phosphate synthase homotetramer in apo form | |||||||||
![]() | Cryptococcus neoformans trehalose-6-phosphate synthase (Tps1) homotetramer in the apo form | |||||||||
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![]() | Glycosyltransferase / complex / transferase | |||||||||
Function / homology | ![]() alpha,alpha-trehalose-phosphate synthase complex (UDP-forming) / trehalose-phosphatase activity / trehalose biosynthetic process / hexosyltransferase activity / trehalose metabolism in response to stress / cellular response to heat / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
![]() | Washington EJ / Brennan RG | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Cryo-EM structure of Cryptococcus neoformans trehalose-6-phosphate synthase homotetramer in apo form Authors: Washington EJ / Brennan RG | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 117.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.5 KB 13.5 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 11.4 KB | Display | ![]() |
Images | ![]() | 111 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() | 115.9 MB 115.9 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.2 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 18.7 KB | Display | |
Data in CIF | ![]() | 24.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8fo1MC 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
File | ![]() | ||||||||||||||||||||
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Annotation | Cryptococcus neoformans trehalose-6-phosphate synthase (Tps1) homotetramer in the apo form | ||||||||||||||||||||
Voxel size | X=Y=Z: 0.65 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: Cryptococcus neoformans trehalose-6-phosphate synthase (Tps1) homotetramer in the...
File | emd_29338_half_map_1.map | ||||||||||||
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Annotation | Cryptococcus neoformans trehalose-6-phosphate synthase (Tps1) homotetramer in the apo half map A | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Cryptococcus neoformans trehalose-6-phosphate synthase (Tps1) homotetramer in the...
File | emd_29338_half_map_2.map | ||||||||||||
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Annotation | Cryptococcus neoformans trehalose-6-phosphate synthase (Tps1) homotetramer in the apo half map B | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : trehalose-6-phosphate synthase homotetramer in apo form
Entire | Name: trehalose-6-phosphate synthase homotetramer in apo form |
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Components |
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-Supramolecule #1: trehalose-6-phosphate synthase homotetramer in apo form
Supramolecule | Name: trehalose-6-phosphate synthase homotetramer in apo form type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 307 KDa |
-Macromolecule #1: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)
Macromolecule | Name: Alpha,alpha-trehalose-phosphate synthase (UDP-forming) type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 76.8155 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MHHHHHHSSG VDLGTENLYF QSNAMTTMSN DIPNSPTSTS FTGTFSPAAT AANTAANART SDAPSPTTSS SGPKLETSKE QRLIVVSNR LPVTISKDDN GEYHFKMSSG GLVSALSGCK KTMSFTWIGW PGKDIPMQDR ETVNRRLLDE YNCYPVYLSD E LADSHYNG ...String: MHHHHHHSSG VDLGTENLYF QSNAMTTMSN DIPNSPTSTS FTGTFSPAAT AANTAANART SDAPSPTTSS SGPKLETSKE QRLIVVSNR LPVTISKDDN GEYHFKMSSG GLVSALSGCK KTMSFTWIGW PGKDIPMQDR ETVNRRLLDE YNCYPVYLSD E LADSHYNG FSNSILWPLF HYHPGEMNFD AAHWLAYREA NMRFADVVSS LVQAGDMVWV QDYHLMLLPM LLRSMITGES AQ GEMVRQE LGRVKEGVDD TVVKEVLKMG PGVAQAEDEG VEMLDDVEEE GGEMDVKSSP KRPHYARGMS TFQKQELVAK EKG KEGIRI GFFLHTPFPS SEIYRILPVR REILLGVLQC DLIGFHTYDY ARHFLSSCTR ILGLETQPNG IEFDGRYCQV GTFP IGIDP NQFIEGLQKE SIVKRLRSLE ARFEGVKVII GVDRLDYIKG IPQKLQALET FLTQHPEWIG KVVLVQLAIP SRQDV EEYQ DLRACVNELV GRINGRFGTV ESVPIHYMHK SVPFEELTAM YALADACLVT STRDGMNLVA YEYISSQAER HGSMIL SEF AGAAQSFNGS LLINPWDVQS TADAINQALT LSPQQRKTNW QKLFNYVSKY TAEAWGVSFV NELNRLSGQR PSGPTGL AG RRKSGSLSRT SSKASIQRRK SSQSGIVTGL GAAAGAAVNW AQAQVQGGSQ T UniProtKB: Alpha,alpha-trehalose-phosphate synthase (UDP-forming) |
-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: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |