4jpo
From Proteopedia
(Difference between revisions)
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| - | + | ==5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1== | |
| - | + | <StructureSection load='4jpo' size='340' side='right' caption='[[4jpo]], [[Resolution|resolution]] 5.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4jpo]] is a 4 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=4JPO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JPO FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSM3, YBR272C, YBR1740 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), RPT1, CIM5, YTA3, YKL145W ([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=4jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jpo RCSB], [http://www.ebi.ac.uk/pdbsum/4jpo PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/HSM3_YEAST HSM3_YEAST]] Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC).<ref>PMID:9539417</ref> <ref>PMID:10681182</ref> <ref>PMID:10681183</ref> <ref>PMID:15450405</ref> <ref>PMID:19446322</ref> <ref>PMID:19217412</ref> <ref>PMID:19412159</ref> [[http://www.uniprot.org/uniprot/PRS7_YEAST PRS7_YEAST]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). | [[http://www.uniprot.org/uniprot/HSM3_YEAST HSM3_YEAST]] Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC).<ref>PMID:9539417</ref> <ref>PMID:10681182</ref> <ref>PMID:10681183</ref> <ref>PMID:15450405</ref> <ref>PMID:19446322</ref> <ref>PMID:19217412</ref> <ref>PMID:19412159</ref> [[http://www.uniprot.org/uniprot/PRS7_YEAST PRS7_YEAST]] The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric alpha-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the alpha-ring. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit. Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound alpha-pockets with poor specificity, except for Rpt6, which uniquely bound the alpha2/alpha3-pocket. Although the Rpt6 tail is not visualized within an alpha-pocket in mature proteasomes, it inserts into the alpha2/alpha3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. | ||
| - | + | Reconfiguration of the proteasome during chaperone-mediated assembly.,Park S, Li X, Kim HM, Singh CR, Tian G, Hoyt MA, Lovell S, Battaile KP, Zolkiewski M, Coffino P, Roelofs J, Cheng Y, Finley D Nature. 2013 May 23;497(7450):512-6. doi: 10.1038/nature12123. Epub 2013 May 5. PMID:23644457<ref>PMID:23644457</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: Battaile, K P | + | [[Category: Battaile, K P]] |
| - | [[Category: Lovell, S | + | [[Category: Lovell, S]] |
| - | [[Category: Roelofs, J | + | [[Category: Roelofs, J]] |
| - | [[Category: Singh, R | + | [[Category: Singh, R]] |
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Chaperone-hydrolase complex]] | [[Category: Chaperone-hydrolase complex]] | ||
Revision as of 20:11, 24 December 2014
5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1
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