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Originally published In Press as doi:10.1074/jbc.M208148200 on November 27, 2002
J. Biol. Chem., Vol. 278, Issue 8, 6543-6551, February 21, 2003
Crystal Structure of the Protease Domain of a
Heat-shock Protein HtrA from Thermotoga maritima*
Dong Young
Kim ,
Dong Ryoung
Kim ,
Sung Chul
Ha ,
Neratur K.
Lokanath ,
Chang Jun
Lee§,
Hye-Yeon
Hwang¶, and
Kyeong Kyu
Kim
From the Department of Molecular Cell Biology, Center
for Molecular Medicine, SBRI, Sungkyunkwan University School of
Medicine, Suwon 440-746, Korea, the § Bioneer Corporation,
49-3, Daejeon 306-220, Korea, and ¶ PENGEN Biotech, R&D Center,
KSBC, Suwon 442-270, Korea
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
NH2-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.
*
This work was supported by Korea Research Foundation Grant
KRF-2000-015-FS0003.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
The atomic coordinates and the structure factors (code 1L1J) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).
To whom correspondence should be addressed. Tel.:
82-31-299-6136; Fax: 82-31-299-6159; E-mail:
kkim@med.skku.ac.kr.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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