2ce3

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[[Image:2ce3.png|left|200px]]
 
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==CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS==
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The line below this paragraph, containing "STRUCTURE_2ce3", creates the "Structure Box" on the page.
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<StructureSection load='2ce3' size='340' side='right'caption='[[2ce3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ce3]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CE3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ce3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ce3 OCA], [https://pdbe.org/2ce3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ce3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ce3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ce3 ProSAT]</span></td></tr>
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{{STRUCTURE_2ce3| PDB=2ce3 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CLPP1_MYCTU CLPP1_MYCTU] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/2ce3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2ce3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Mycobacterium tuberculosis caseinolytic protease ClpP1 (Mt ClpP1) is a self-compartmentalized protease consisting of two heptameric rings stacked on top of each other, thus enclosing a catalytic chamber. Within the chamber, which can be reached through two axial pores, each of the 14 identical monomers possesses a serine protease active site. The unfolding and translocation of substrates into the chamber are mediated by associated hexameric ATPases covering the axial pores. Three crystal structures of Mt ClpP1, determined by molecular replacement, are presented in this study. Two of the models were refined to a resolution of 2.6 A and the third to 3.0 A. It was found that disorder in the handle domain affects the formation and configuration of the tetradecamer and results in condensed structures with larger equatorial pores when compared with ClpPs from other species. Additionally, this disorder accompanies conformational changes of the residues in the catalytic triad. The models also reveal structural differences within the N-terminal hairpin-loop domain, which possibly reflect the significant differences in amino-acid sequence between Mt ClpP1 and other ClpP homologues in this region.
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===CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS===
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Insights into the inter-ring plasticity of caseinolytic proteases from the X-ray structure of Mycobacterium tuberculosis ClpP1.,Ingvarsson H, Mate MJ, Hogbom M, Portnoi D, Benaroudj N, Alzari PM, Ortiz-Lombardia M, Unge T Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):249-59. Epub 2007, Jan 16. PMID:17242518<ref>PMID:17242518</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ce3" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17242518}}, adds the Publication Abstract to the page
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*[[Clp protease 3D structures|Clp protease 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17242518 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17242518}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2CE3 is a 14 chains structure of sequences from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CE3 OCA].
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Alzari PM]]
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==Reference==
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[[Category: Kim CY]]
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<ref group="xtra">PMID:17242518</ref><references group="xtra"/>
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[[Category: Lekin T]]
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[[Category: Endopeptidase Clp]]
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[[Category: Ortiz-Lombardia M]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Segelke B]]
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[[Category: Alzari, P M.]]
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[[Category: Kim, C Y.]]
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[[Category: Lekin, T.]]
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[[Category: Ortiz-Lombardia, M.]]
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[[Category: Segelke, B.]]
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[[Category: Atp-dependent protease]]
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[[Category: Clp protease]]
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[[Category: Endopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Proteolytic subunit]]
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[[Category: Serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:40:58 2009''
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Current revision

CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS

PDB ID 2ce3

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