1jhe
From Proteopedia
(New page: 200px<br /><applet load="1jhe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jhe, resolution 2.5Å" /> '''LEXA L89P Q92W E152A ...) |
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| - | [[Image:1jhe.jpg|left|200px]]<br /><applet load="1jhe" size=" | + | [[Image:1jhe.jpg|left|200px]]<br /><applet load="1jhe" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jhe, resolution 2.5Å" /> | caption="1jhe, resolution 2.5Å" /> | ||
'''LEXA L89P Q92W E152A K156A MUTANT'''<br /> | '''LEXA L89P Q92W E152A K156A MUTANT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction | + | LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction requires an activated form of RecA, but it occurs spontaneously in vitro at high pH. Accordingly, LexA must both allow self-cleavage and yet prevent this reaction in the absence of a stimulus. We have solved the crystal structures of several mutant forms of LexA. Strikingly, two distinct conformations are observed, one compatible with cleavage, and the other in which the cleavage site is approximately 20 A from the catalytic center. Our analysis provides insight into the structural and energetic features that modulate the interconversion between these two forms and hence the rate of the self-cleavage reaction. We suggest RecA activates the self-cleavage of LexA and related proteins through selective stabilization of the cleavable conformation. |
==About this Structure== | ==About this Structure== | ||
| - | 1JHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Repressor_lexA Repressor lexA], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.88 3.4.21.88] Full crystallographic information is available from [http:// | + | 1JHE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Repressor_lexA Repressor lexA], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.88 3.4.21.88] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Repressor lexA]] | [[Category: Repressor lexA]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Little, J | + | [[Category: Little, J W.]] |
[[Category: Luo, Y.]] | [[Category: Luo, Y.]] | ||
[[Category: Mosimann, S.]] | [[Category: Mosimann, S.]] | ||
| - | [[Category: Pfuetzner, R | + | [[Category: Pfuetzner, R A.]] |
| - | [[Category: Strynadka, N | + | [[Category: Strynadka, N C.J.]] |
[[Category: c-terminal]] | [[Category: c-terminal]] | ||
[[Category: lexa sos repressor]] | [[Category: lexa sos repressor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:22:40 2008'' |
Revision as of 11:22, 21 February 2008
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LEXA L89P Q92W E152A K156A MUTANT
Overview
LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction requires an activated form of RecA, but it occurs spontaneously in vitro at high pH. Accordingly, LexA must both allow self-cleavage and yet prevent this reaction in the absence of a stimulus. We have solved the crystal structures of several mutant forms of LexA. Strikingly, two distinct conformations are observed, one compatible with cleavage, and the other in which the cleavage site is approximately 20 A from the catalytic center. Our analysis provides insight into the structural and energetic features that modulate the interconversion between these two forms and hence the rate of the self-cleavage reaction. We suggest RecA activates the self-cleavage of LexA and related proteins through selective stabilization of the cleavable conformation.
About this Structure
1JHE is a Single protein structure of sequence from Escherichia coli. Active as Repressor lexA, with EC number 3.4.21.88 Full crystallographic information is available from OCA.
Reference
Crystal structure of LexA: a conformational switch for regulation of self-cleavage., Luo Y, Pfuetzner RA, Mosimann S, Paetzel M, Frey EA, Cherney M, Kim B, Little JW, Strynadka NC, Cell. 2001 Sep 7;106(5):585-94. PMID:11551506
Page seeded by OCA on Thu Feb 21 13:22:40 2008
