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2z5e

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Revision as of 02:22, 25 December 2014

Crystal Structure of Proteasome Assembling Chaperone 3

Structural highlights

2z5e is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PSMG3_HUMAN] Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled.

Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes.,Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hirano Y, Hayashi H, Iemura S, Hendil KB, Niwa S, Kishimoto T, Kasahara M, Natsume T, Tanaka K, Murata S. Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes. Mol Cell. 2006 Dec 28;24(6):977-84. PMID:17189198 doi:http://dx.doi.org/10.1016/j.molcel.2006.11.015
↑ Yashiroda H, Mizushima T, Okamoto K, Kameyama T, Hayashi H, Kishimoto T, Niwa S, Kasahara M, Kurimoto E, Sakata E, Takagi K, Suzuki A, Hirano Y, Murata S, Kato K, Yamane T, Tanaka K. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes. Nat Struct Mol Biol. 2008 Mar;15(3):228-36. Epub 2008 Feb 17. PMID:18278057 doi:http://dx.doi.org/10.1038/nsmb.1386

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2z5e"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2z5e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Z5E FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2z5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z5e RCSB], [http://www.ebi.ac.uk/pdbsum/2z5e PDBsum]</span></td></tr>
+</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=2z5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z5e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2z5e RCSB], [http://www.ebi.ac.uk/pdbsum/2z5e PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PSMG3_HUMAN PSMG3_HUMAN]] Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes.<ref>PMID:17189198</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 30: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Hirano, Y.]]
+[[Category: Hirano, Y]]
-[[Category: Kato, K.]]
+[[Category: Kato, K]]
-[[Category: Kurimoto, E.]]
+[[Category: Kurimoto, E]]
-[[Category: Murata, S.]]
+[[Category: Murata, S]]
-[[Category: Okamoto, K.]]
+[[Category: Okamoto, K]]
-[[Category: Sakata, E.]]
+[[Category: Sakata, E]]
-[[Category: Suzuki, A.]]
+[[Category: Suzuki, A]]
-[[Category: Tanaka, K.]]
+[[Category: Tanaka, K]]
-[[Category: Yamane, T.]]
+[[Category: Yamane, T]]
 [[Category: Beta sandwich]]
 [[Category: Chaperone]]
 [[Category: Homodimer]]
 [[Category: Proteasome]]

2z5e

From Proteopedia

Revision as of 02:22, 25 December 2014

Crystal Structure of Proteasome Assembling Chaperone 3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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