2ce3

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[[Image:2ce3.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS==
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|PDB= 2ce3 |SIZE=350|CAPTION= <scene name='initialview01'>2ce3</scene>, resolution 2.596&Aring;
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<StructureSection load='2ce3' size='340' side='right'caption='[[2ce3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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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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|ACTIVITY= [http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92]
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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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|GENE=
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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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}}
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</table>
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== Function ==
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'''CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS'''
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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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==Overview==
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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 ==
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.
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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==About this Structure==
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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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2CE3 is a [[Single protein]] structure of sequence 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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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17242518 17242518]
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</div>
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[[Category: Endopeptidase Clp]]
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<div class="pdbe-citations 2ce3" style="background-color:#fffaf0;"></div>
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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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 Thu Mar 20 16:14:15 2008''
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==See Also==
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*[[Clp protease 3D structures|Clp protease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Alzari PM]]
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[[Category: Kim CY]]
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[[Category: Lekin T]]
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[[Category: Ortiz-Lombardia M]]
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[[Category: Segelke B]]

Current revision

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

PDB ID 2ce3

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