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2h6j

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Revision as of 08:07, 18 October 2017

Crystal Structure of the Beta F145A Rhodococcus Proteasome

Structural highlights

2h6j is a 14 chain structure with sequence from "mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	prcA 1 ("Mycobacterium erythropolis" Gray and Thornton 1928), prcB 1 ("Mycobacterium erythropolis" Gray and Thornton 1928)
Activity:	Proteasome endopeptidase complex, with EC number 3.4.25.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PSA1_RHOER] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.[HAMAP-Rule:MF_00289]^[1] ^[2] [PSB1_RHOER] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activity but no caspase-like activity.[HAMAP-Rule:MF_02113]^[3] ^[4]

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

The processing of propeptides and the maturation of 20S proteasomes require the association of beta rings from two half proteasomes. We propose an assembly-dependent activation model in which interactions between helix (H3 and H4) residues of the opposing half proteasomes are prerequisite for appropriate positioning of the S2-S3 loop; such positioning enables correct coordination of the active-site residue needed for propeptide cleavage. Mutations of H3 or H4 residues that participate in the association of two half proteasomes inhibit activation and prevent, in nearly all cases, the formation of full proteasomes. In contrast, mutations affecting interactions with residues of the S2-S3 loop allow the assembly of full, but activity impacted, proteasomes. The crystal structure of the inactive H3 mutant, Phe145Ala, shows that the S2-S3 loop is displaced from the position observed in wild-type proteasomes. These data support the proposed assembly-dependent activation model in which the S2-S3 loop acts as an activation switch.

Proteasome assembly triggers a switch required for active-site maturation.,Witt S, Kwon YD, Sharon M, Felderer K, Beuttler M, Robinson CV, Baumeister W, Jap BK Structure. 2006 Jul;14(7):1179-88. PMID:16843899^[5]

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

References

↑ Tamura T, Nagy I, Lupas A, Lottspeich F, Cejka Z, Schoofs G, Tanaka K, De Mot R, Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr Biol. 1995 Jul 1;5(7):766-74. PMID:7583123
↑ Zuhl F, Tamura T, Dolenc I, Cejka Z, Nagy I, De Mot R, Baumeister W. Subunit topology of the Rhodococcus proteasome. FEBS Lett. 1997 Jan 2;400(1):83-90. PMID:9000518
↑ Tamura T, Nagy I, Lupas A, Lottspeich F, Cejka Z, Schoofs G, Tanaka K, De Mot R, Baumeister W. The first characterization of a eubacterial proteasome: the 20S complex of Rhodococcus. Curr Biol. 1995 Jul 1;5(7):766-74. PMID:7583123
↑ Zuhl F, Tamura T, Dolenc I, Cejka Z, Nagy I, De Mot R, Baumeister W. Subunit topology of the Rhodococcus proteasome. FEBS Lett. 1997 Jan 2;400(1):83-90. PMID:9000518
↑ Witt S, Kwon YD, Sharon M, Felderer K, Beuttler M, Robinson CV, Baumeister W, Jap BK. Proteasome assembly triggers a switch required for active-site maturation. Structure. 2006 Jul;14(7):1179-88. PMID:16843899 doi:10.1016/j.str.2006.05.019

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/2h6j"

@@ Line 1: / Line 1: @@
-==Crystal Structure of the Beta F145A Rhodococcus Proteasome (CASP Target)==
+==Crystal Structure of the Beta F145A Rhodococcus Proteasome==
 <StructureSection load='2h6j' size='340' side='right' caption='[[2h6j]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prcA 1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928]), prcB 1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></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=2h6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6j OCA], [http://pdbe.org/2h6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h6j RCSB], [http://www.ebi.ac.uk/pdbsum/2h6j PDBsum]</span></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=2h6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6j OCA], [http://pdbe.org/2h6j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h6j RCSB], [http://www.ebi.ac.uk/pdbsum/2h6j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h6j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2h6j" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Proteasome|Proteasome]]
 == References ==
 <references/>

2h6j

From Proteopedia

Revision as of 08:07, 18 October 2017

Crystal Structure of the Beta F145A Rhodococcus Proteasome

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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