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3vlf

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Revision as of 18:51, 27 July 2022

Crystal structure of yeast proteasome interacting protein

Structural highlights

3vlf is a 4 chain structure with sequence from Baker's yeast. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	3vld, 3vle
Gene:	HSM3, YBR272C, YBR1740 (Baker's yeast), RPT1, CIM5, YTA3, YKL145W (Baker's yeast)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] [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).

Publication Abstract from PubMed

The 26 S proteasome is a 2.5-MDa molecular machine that degrades ubiquitinated proteins in eukaryotic cells. It consists of a proteolytic core particle and two 19 S regulatory particles (RPs) composed of 6 ATPase (Rpt) and 13 non-ATPase (Rpn) subunits. Multiple proteasome-dedicated chaperones facilitate the assembly of the proteasome, but little is known about the detailed mechanisms. Hsm3, a 19 S RP dedicated chaperone, transiently binds to the C-terminal domain of the Rpt1 subunit and forms a tetrameric complex, Hsm3-Rpt1-Rpt2-Rpn1, during maturation of the ATPase ring of 19 S RP. To elucidate the structural basis of Hsm3 function, we determined the crystal structures of Hsm3 and its complex with the C-terminal domain of the Rpt1 subunit (Rpt1C). Hsm3 has a C-shaped structure that consists of 11 HEAT repeats. The structure of the Hsm3-Rpt1C complex revealed that the interacting surface between Hsm3 and Rpt1 is a hydrophobic core and a complementary charged surface. Mutations in the Hsm3-Rpt1 surface resulted in the assembly defect of the 26 S proteasome. Furthermore, a structural model of the Hsm3-Rpt ring complex and an in vitro binding assay suggest that Hsm3 can bind Rpt2 in addition to Rpt1. Collectively, our results provide the structural basis of the molecular functions of Hsm3 for the RP assembly.

Structural Basis for Specific Recognition of Rpt1p, an ATPase Subunit of 26 S Proteasome, by Proteasome-dedicated Chaperone Hsm3p.,Takagi K, Kim S, Yukii H, Ueno M, Morishita R, Endo Y, Kato K, Tanaka K, Saeki Y, Mizushima T J Biol Chem. 2012 Apr 6;287(15):12172-82. Epub 2012 Feb 8. PMID:22334676^[8]

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

References

↑ Fedorova IV, Gracheva LM, Kovaltzova SV, Evstuhina TA, Alekseev SY, Korolev VG. The yeast HSM3 gene acts in one of the mismatch repair pathways. Genetics. 1998 Mar;148(3):963-73. PMID:9539417
↑ Merker JD, Datta A, Kolodner RD, Petes TD. The yeast HSM3 gene is not involved in DNA mismatch repair in rapidly dividing cells. Genetics. 2000 Jan;154(1):491-3. PMID:10681182
↑ Fedorova IV, Kovaltzova SV, Korolev VG. The yeast HSM3 gene is involved in DNA mismatch repair in slowly dividing cells. Genetics. 2000 Jan;154(1):495-6. PMID:10681183
↑ Fedorova IV, Kovaltzova SV, Gracheva LM, Evstuhina TA, Korolev VG. Requirement of HSM3 gene for spontaneous mutagenesis in Saccharomyces cerevisiae. Mutat Res. 2004 Oct 4;554(1-2):67-75. PMID:15450405 doi:10.1016/j.mrfmmm.2004.03.003
↑ Funakoshi M, Tomko RJ Jr, Kobayashi H, Hochstrasser M. Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell. 2009 May 29;137(5):887-99. Epub 2009 May 14. PMID:19446322 doi:S0092-8674(09)00526-1
↑ Le Tallec B, Barrault MB, Guerois R, Carre T, Peyroche A. Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome. Mol Cell. 2009 Feb 13;33(3):389-99. doi: 10.1016/j.molcel.2009.01.010. PMID:19217412 doi:10.1016/j.molcel.2009.01.010
↑ Roelofs J, Park S, Haas W, Tian G, McAllister FE, Huo Y, Lee BH, Zhang F, Shi Y, Gygi SP, Finley D. Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature. 2009 Jun 11;459(7248):861-5. PMID:19412159 doi:nature08063
↑ Takagi K, Kim S, Yukii H, Ueno M, Morishita R, Endo Y, Kato K, Tanaka K, Saeki Y, Mizushima T. Structural Basis for Specific Recognition of Rpt1p, an ATPase Subunit of 26 S Proteasome, by Proteasome-dedicated Chaperone Hsm3p. J Biol Chem. 2012 Apr 6;287(15):12172-82. Epub 2012 Feb 8. PMID:22334676 doi:10.1074/jbc.M112.345876

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vlf"

@@ Line 1: / Line 1: @@
 ==Crystal structure of yeast proteasome interacting protein==
-<StructureSection load='3vlf' size='340' side='right' caption='[[3vlf]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<StructureSection load='3vlf' size='340' side='right'caption='[[3vlf]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vlf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VLF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vlf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VLF FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vld|3vld]], [[3vle|3vle]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vld|3vld]], [[3vle|3vle]]</div></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 Baker's yeast]), RPT1, CIM5, YTA3, YKL145W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSM3, YBR272C, YBR1740 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), RPT1, CIM5, YTA3, YKL145W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3vlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vlf OCA], [http://pdbe.org/3vlf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vlf RCSB], [http://www.ebi.ac.uk/pdbsum/3vlf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vlf ProSAT]</span></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=3vlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vlf OCA], [https://pdbe.org/3vlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vlf RCSB], [https://www.ebi.ac.uk/pdbsum/3vlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vlf ProSAT]</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).
+[[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>  [[https://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 ==
@@ Line 22: / Line 22: @@
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
 == References ==
 <references/>
@@ Line 28: / Line 29: @@
 </StructureSection>
 [[Category: Baker's yeast]]
+[[Category: Large Structures]]
 [[Category: Kato, K]]
 [[Category: Kim, S]]

3vlf

From Proteopedia

Revision as of 18:51, 27 July 2022

Crystal structure of yeast proteasome interacting protein

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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