1eo6

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Current revision (07:05, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1eo6' size='340' side='right'caption='[[1eo6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1eo6' size='340' side='right'caption='[[1eo6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1eo6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. 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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<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 ==
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[[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>
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[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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1eo6" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bovin]]
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[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Elazar, Z]]
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[[Category: Elazar Z]]
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[[Category: Fass, D]]
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[[Category: Fass D]]
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[[Category: Paz, Y]]
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[[Category: Paz Y]]
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[[Category: Protein binding]]
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[[Category: Ubiquitin fold]]
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Current revision

CRYSTAL STRUCTURE OF GATE-16

PDB ID 1eo6

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