3ruj
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal Structure of N-terminal region of yeast Atg7== | |
| - | + | <StructureSection load='3ruj' size='340' side='right' caption='[[3ruj]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3ruj]] is a 1 chain structure with sequence from [http://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=3RUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RUJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rui|3rui]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATG7, APG7, CVT2, YHR171W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ruj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ruj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ruj RCSB], [http://www.ebi.ac.uk/pdbsum/3ruj PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Autophagy is the degradation of cellular organelles via the lysosomal pathway. The autophagic ubiquitin-like (Ubl) molecule Atg8 is activated by the E1-like enzyme Atg7. As this noncanonical E1 enzyme's domain organization is unique among Ubl-activating E1 enzymes, the structural basis for its interactions with Atg8 and partner E2 enzymes remains obscure. Here we present the structure of the N-terminal domain of Atg7, revealing a unique protein fold and interactions with both autophagic E2 enzymes Atg3 and Atg10. The structure of the C-terminal domain of Atg7 in complex with Atg8 shows the mode of dimerization and mechanism of recognition of Atg8. Notably, the catalytic cysteine residue in Atg7 is positioned close to the C-terminal glycine of Atg8, its target for thioester formation, potentially eliminating the need for large conformational rearrangements characteristic of other E1s. | ||
| - | + | Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8.,Hong SB, Kim BW, Lee KE, Kim SW, Jeon H, Kim J, Song HK Nat Struct Mol Biol. 2011 Nov 6. doi: 10.1038/nsmb.2165. PMID:22056771<ref>PMID:22056771</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
| - | [[Category: Hong, S B | + | [[Category: Hong, S B]] |
| - | [[Category: Kim, B W | + | [[Category: Kim, B W]] |
| - | [[Category: Song, H K | + | [[Category: Song, H K]] |
[[Category: Atg10]] | [[Category: Atg10]] | ||
[[Category: Atg3]] | [[Category: Atg3]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Protein transport]] | [[Category: Protein transport]] | ||
Revision as of 11:00, 19 December 2014
Crystal Structure of N-terminal region of yeast Atg7
| |||||||||||
