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[[Image:2h6j.gif|left|200px]]
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{{STRUCTURE_2h6j|  PDB=2h6j  |  SCENE=  }}
'''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 ==
<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='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='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>
</table>
== Function ==
[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>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2h6j ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:16843899</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2H6J is a [[Protein complex]] structure of sequences from [http://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].
</div>
<div class="pdbe-citations 2h6j" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/16843899 16843899]
*[[Proteasome 3D structures|Proteasome 3D structures]]
[[Category: Proteasome endopeptidase complex]]
== References ==
[[Category: Protein complex]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus erythropolis]]
[[Category: Rhodococcus erythropolis]]
[[Category: Kwon, Y D.]]
[[Category: Kwon YD]]
[[Category: 20s proteasome]]
[[Category: Assembly-dependent activation]]
[[Category: Half proteasome]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:55:39 2008''
Retrieved from "https://proteopedia.org/2h6j"