This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5fd9
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| + | |||
==X-ray Crystal Structure of ESCRT-III Snf7 core domain (conformation B)== | ==X-ray Crystal Structure of ESCRT-III Snf7 core domain (conformation B)== | ||
| - | <StructureSection load='5fd9' size='340' side='right' caption='[[5fd9]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='5fd9' size='340' side='right'caption='[[5fd9]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5fd9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FD9 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5fd9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FD9 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fd9 OCA], [https://pdbe.org/5fd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fd9 RCSB], [https://www.ebi.ac.uk/pdbsum/5fd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fd9 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/SNF7_YEAST SNF7_YEAST] Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Appears to sequester MVB cargo. Recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles.<ref>PMID:11559748</ref> <ref>PMID:12194857</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: | + | [[Category: Borbat PP]] |
| - | [[Category: | + | [[Category: Buchkovich NJ]] |
| - | [[Category: | + | [[Category: Emr SD]] |
| - | [[Category: | + | [[Category: Freed JH]] |
| - | [[Category: | + | [[Category: Fromme JC]] |
| - | [[Category: | + | [[Category: Henne WM]] |
| - | [[Category: | + | [[Category: Mao Y]] |
| - | [[Category: | + | [[Category: Tang S]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
X-ray Crystal Structure of ESCRT-III Snf7 core domain (conformation B)
| |||||||||||
