4jpo

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:46, 20 September 2023) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_4jpo| PDB=4jpo | SCENE= }}
 
-
===5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1===
 
-
{{ABSTRACT_PUBMED_23644457}}
 
-
==Function==
+
==5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1==
-
[[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).
+
<StructureSection load='4jpo' size='340' side='right'caption='[[4jpo]], [[Resolution|resolution]] 5.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4jpo]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4JPO FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5&#8491;</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=4jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jpo OCA], [https://pdbe.org/4jpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jpo RCSB], [https://www.ebi.ac.uk/pdbsum/4jpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jpo ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://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>
 +
<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.
-
==About this Structure==
+
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>
-
[[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].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:023644457</ref><references group="xtra"/><references/>
+
</div>
-
[[Category: Saccharomyces cerevisiae s288c]]
+
<div class="pdbe-citations 4jpo" style="background-color:#fffaf0;"></div>
-
[[Category: Battaile, K P.]]
+
 
-
[[Category: Lovell, S.]]
+
==See Also==
-
[[Category: Roelofs, J.]]
+
*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]]
-
[[Category: Singh, R.]]
+
== References ==
-
[[Category: Chaperone]]
+
<references/>
-
[[Category: Chaperone-hydrolase complex]]
+
__TOC__
-
[[Category: Hsm3]]
+
</StructureSection>
-
[[Category: Proteasome]]
+
[[Category: Large Structures]]
-
[[Category: Protein complex]]
+
[[Category: Saccharomyces cerevisiae S288C]]
 +
[[Category: Battaile KP]]
 +
[[Category: Lovell S]]
 +
[[Category: Roelofs J]]
 +
[[Category: Singh R]]

Current revision

5A resolution structure of Proteasome Assembly Chaperone Hsm3 in complex with a C-terminal fragment of Rpt1

PDB ID 4jpo

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4jpo"
Personal tools