1l1j

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[[Image:1l1j.jpg|left|200px]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l1j OCA], [http://www.ebi.ac.uk/pdbsum/1l1j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l1j RCSB]</span>
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'''Crystal structure of the protease domain of an ATP-independent heat shock protease HtrA'''
'''Crystal structure of the protease domain of an ATP-independent heat shock protease HtrA'''
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[[Category: Kim, K K.]]
[[Category: Kim, K K.]]
[[Category: Lokanath, N K.]]
[[Category: Lokanath, N K.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine proteinase]]
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[[Category: Serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:26:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:45 2008''
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Revision as of 20:26, 2 May 2008

Template:STRUCTURE 1l1j

Crystal structure of the protease domain of an ATP-independent heat shock protease HtrA


Overview

HtrA (high temperature requirement A), a periplasmic heat-shock protein, functions as a molecular chaperone at low temperatures, and its proteolytic activity is turned on at elevated temperatures. To investigate the mechanism of functional switch to protease, we determined the crystal structure of the NH(2)-terminal protease domain (PD) of HtrA from Thermotoga maritima, which was shown to retain both proteolytic and chaperone-like activities. Three subunits of HtrA PD compose a trimer, and multimerization architecture is similar to that found in the crystal structures of intact HtrA hexamer from Escherichia coli and human HtrA2 trimer. HtrA PD shares the same fold with chymotrypsin-like serine proteases, but it contains an additional lid that blocks access the of substrates to the active site. A corresponding lid found in E. coli HtrA is a long loop that also blocks the active site of another subunit. These results suggest that the activation of the proteolytic function of HtrA at elevated temperatures might occur by a conformational change, which includes the opening of the helical lid to expose the active site and subsequent rearrangement of a catalytic triad and an oxyanion hole.

About this Structure

1L1J is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima., Kim DY, Kim DR, Ha SC, Lokanath NK, Lee CJ, Hwang HY, Kim KK, J Biol Chem. 2003 Feb 21;278(8):6543-51. Epub 2002 Nov 27. PMID:12458220 Page seeded by OCA on Fri May 2 23:26:06 2008

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