1eo6
From Proteopedia
(Difference between revisions)
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<StructureSection load='1eo6' size='340' side='right'caption='[[1eo6]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1eo6' size='340' side='right'caption='[[1eo6]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1eo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1eo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EO6 FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo6 OCA], [https://pdbe.org/1eo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1eo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eo6 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eo6 OCA], [https://pdbe.org/1eo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1eo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eo6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/GBRL2_BOVIN GBRL2_BOVIN] Involved in autophagy (By similarity). Involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1.<ref>PMID:10747018</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eo6 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eo6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The GATE-16 protein participates in intra-Golgi transport and can associate with the N-ethylmaleimide-sensitive fusion protein and with Golgi SNAREs. The yeast ortholog of GATE-16 is the autophagocytosis factor Aut7p. GATE-16 is also closely related to the GABA receptor-associated protein (GABARAP), which has been proposed to cluster neurotransmitter receptors by mediating interaction with the cytoskeleton, and to the light chain-3 subunit of the neuronal microtubule-associated protein complex. Here, we present the crystal structure of GATE-16 refined to 1.8 A resolution. GATE-16 contains a ubiquitin fold decorated by two additional N-terminal helices. Proteins with strong structural similarity but no detectable sequence homology to GATE-16 include Ras effectors that mediate diverse downstream functions, but each interacts with Ras by forming pseudo-continuous beta-sheets. The GATE-16 surface suggests that it binds its targets in a similar manner. Moreover, a second potential protein-protein interaction site on GATE-16 may explain the adapter activity observed for members of the GATE-16 family. | ||
- | |||
- | Structure of GATE-16, membrane transport modulator and mammalian ortholog of autophagocytosis factor Aut7p.,Paz Y, Elazar Z, Fass D J Biol Chem. 2000 Aug 18;275(33):25445-50. PMID:10856287<ref>PMID:10856287</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1eo6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Elazar | + | [[Category: Elazar Z]] |
- | [[Category: Fass | + | [[Category: Fass D]] |
- | [[Category: Paz | + | [[Category: Paz Y]] |
- | + | ||
- | + |
Current revision
CRYSTAL STRUCTURE OF GATE-16
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Categories: Bos taurus | Large Structures | Elazar Z | Fass D | Paz Y