2ce3
From Proteopedia
(New page: 200px<br /><applet load="2ce3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ce3, resolution 2.596Å" /> '''CRYSTAL STRUCTURE O...) |
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| - | [[Image:2ce3.gif|left|200px]]<br /><applet load="2ce3" size=" | + | [[Image:2ce3.gif|left|200px]]<br /><applet load="2ce3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ce3, resolution 2.596Å" /> | caption="2ce3, resolution 2.596Å" /> | ||
'''CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS'''<br /> | '''CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Mycobacterium tuberculosis caseinolytic protease ClpP1 (Mt ClpP1) is a | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2CE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [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] Full crystallographic information is available from [http:// | + | 2CE3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CE3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alzari, P | + | [[Category: Alzari, P M.]] |
| - | [[Category: Kim, C | + | [[Category: Kim, C Y.]] |
[[Category: Lekin, T.]] | [[Category: Lekin, T.]] | ||
[[Category: Ortiz-Lombardia, M.]] | [[Category: Ortiz-Lombardia, M.]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:47:40 2008'' |
Revision as of 14:47, 21 February 2008
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CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS
Overview
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.
About this Structure
2CE3 is a Single protein structure of sequence from Mycobacterium tuberculosis. Active as Endopeptidase Clp, with EC number 3.4.21.92 Full crystallographic information is available from OCA.
Reference
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
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