1zb1
From Proteopedia
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<StructureSection load='1zb1' size='340' side='right'caption='[[1zb1]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='1zb1' size='340' side='right'caption='[[1zb1]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1zb1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1zb1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZB1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZB1 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=1zb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zb1 OCA], [https://pdbe.org/1zb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zb1 RCSB], [https://www.ebi.ac.uk/pdbsum/1zb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zb1 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]] 1.95Å</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=1zb1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zb1 OCA], [https://pdbe.org/1zb1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zb1 RCSB], [https://www.ebi.ac.uk/pdbsum/1zb1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zb1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/BRO1_YEAST BRO1_YEAST] Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p-mitogen-activated protein kinase pathway.<ref>PMID:8649366</ref> <ref>PMID:11454748</ref> <ref>PMID:12062418</ref> <ref>PMID:12668726</ref> <ref>PMID:14523026</ref> <ref>PMID:15326198</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=1zb1 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=1zb1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Proteins delivered to the lysosome or the yeast vacuole via late endosomes are sorted by the ESCRT complexes and by associated proteins, including Alix and its yeast homolog Bro1. Alix, Bro1, and several other late endosomal proteins share a conserved 160 residue Bro1 domain whose boundaries, structure, and function have not been characterized. The crystal structure of the Bro1 domain of Bro1 reveals a folded core of 367 residues. The extended Bro1 domain is necessary and sufficient for binding to the ESCRT-III subunit Snf7 and for the recruitment of Bro1 to late endosomes. The structure resembles a boomerang with its concave face filled in and contains a triple tetratricopeptide repeat domain as a substructure. Snf7 binds to a conserved hydrophobic patch on Bro1 that is required for protein complex formation and for the protein-sorting function of Bro1. These results define a conserved mechanism whereby Bro1 domain-containing proteins are targeted to endosomes by Snf7 and its orthologs. | ||
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| - | Structural basis for endosomal targeting by the Bro1 domain.,Kim J, Sitaraman S, Hierro A, Beach BM, Odorizzi G, Hurley JH Dev Cell. 2005 Jun;8(6):937-47. PMID:15935782<ref>PMID:15935782</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1zb1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Beach | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Hierro | + | [[Category: Beach BM]] |
| - | [[Category: Hurley | + | [[Category: Hierro A]] |
| - | [[Category: Kim | + | [[Category: Hurley JH]] |
| - | [[Category: Odorizzi | + | [[Category: Kim J]] |
| - | [[Category: Sitaraman | + | [[Category: Odorizzi G]] |
| - | + | [[Category: Sitaraman S]] | |
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Current revision
Structure basis for endosomal targeting by the Bro1 domain
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