2h6j: Difference between revisions

Latest revision as of 09:52, 30 August 2023

Crystal Structure of the Beta F145A Rhodococcus Proteasome

Structural highlights

2h6j is a 14 chain structure with sequence from Rhodococcus erythropolis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
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]

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^[3]

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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] 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]

[2]

[3]

@@ Line 1: / Line 1: @@
-==Crystal Structure of the Beta F145A Rhodococcus Proteasome (CASP Target)==
-<StructureSection load='2h6j' size='340' side='right' caption='[[2h6j]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+==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 ==
-<table><tr><td colspan='2'>[[2h6j]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H6J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2h6j]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H6J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H6J FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</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'>[https://proteopedia.org/fgij/fg.htm?mol=2h6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6j OCA], [https://pdbe.org/2h6j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h6j RCSB], [https://www.ebi.ac.uk/pdbsum/2h6j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h6j ProSAT]</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>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PSA1_RHOER 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]<ref>PMID:7583123</ref> <ref>PMID:9000518</ref>  [[http://www.uniprot.org/uniprot/PSB1_RHOER 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]<ref>PMID:7583123</ref> <ref>PMID:9000518</ref>
+[https://www.uniprot.org/uniprot/PSA1_RHOER 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]<ref>PMID:7583123</ref> <ref>PMID:9000518</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/2h6j_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/2h6j_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium erythropolis gray and thornton 1928]]
+[[Category: Large Structures]]
-[[Category: Proteasome endopeptidase complex]]
+[[Category: Rhodococcus erythropolis]]
-[[Category: Kwon, Y D]]
+[[Category: Kwon YD]]
-[[Category: 20s proteasome]]
-[[Category: Assembly-dependent activation]]
-[[Category: Half proteasome]]
-[[Category: Hydrolase]]

2h6j: Difference between revisions

Latest revision as of 09:52, 30 August 2023

Crystal Structure of the Beta F145A Rhodococcus Proteasome

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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