1wrd
From Proteopedia
(Difference between revisions)
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<StructureSection load='1wrd' size='340' side='right'caption='[[1wrd]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1wrd' size='340' side='right'caption='[[1wrd]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1wrd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1wrd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WRD 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=1wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrd OCA], [https://pdbe.org/1wrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wrd RCSB], [https://www.ebi.ac.uk/pdbsum/1wrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wrd 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]] 1.75Å</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=1wrd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrd OCA], [https://pdbe.org/1wrd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wrd RCSB], [https://www.ebi.ac.uk/pdbsum/1wrd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wrd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/TOM1_HUMAN TOM1_HUMAN] May be involved in intracellular trafficking. Probable association with membranes. | |
== 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=1wrd 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=1wrd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Tom1 (Target of Myb1) is suggested to be involved in the transport of ubiquitinated proteins, through the interaction of its GAT (GGA and Tom1) domain with ubiquitin. Here, we demonstrate that the three-helix bundle of Tom1-GAT has two ubiquitin-binding sites recognizing the hydrophobic Ile44 surface of ubiquitin. The complex crystal structure demonstrates that the first site is a hydrophobic patch on helices alpha1 and alpha2. NMR and biochemical data revealed that the N-terminal half of helix alpha3 of Tom1-GAT constitutes the second, stronger binding site. The double-sided ubiquitin binding enhances the efficiency of recognition of ubiquitinated proteins by Tom1. | ||
- | |||
- | Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain.,Akutsu M, Kawasaki M, Katoh Y, Shiba T, Yamaguchi Y, Kato R, Kato K, Nakayama K, Wakatsuki S FEBS Lett. 2005 Oct 10;579(24):5385-91. PMID:16199040<ref>PMID:16199040</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1wrd" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[3D structures of ubiquitin|3D structures of ubiquitin]] | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Akutsu | + | [[Category: Akutsu M]] |
- | [[Category: Kato | + | [[Category: Kato K]] |
- | [[Category: Kato | + | [[Category: Kato R]] |
- | [[Category: Katoh | + | [[Category: Katoh Y]] |
- | [[Category: Kawasaki | + | [[Category: Kawasaki M]] |
- | [[Category: Nakayama | + | [[Category: Nakayama K]] |
- | [[Category: Shiba | + | [[Category: Shiba T]] |
- | [[Category: Wakatsuki | + | [[Category: Wakatsuki S]] |
- | [[Category: Yamaguchi | + | [[Category: Yamaguchi Y]] |
- | + | ||
- | + | ||
- | + |
Current revision
Crystal structure of Tom1 GAT domain in complex with ubiquitin
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Categories: Bos taurus | Homo sapiens | Large Structures | Akutsu M | Kato K | Kato R | Katoh Y | Kawasaki M | Nakayama K | Shiba T | Wakatsuki S | Yamaguchi Y