1jhh

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(New page: 200px<br /><applet load="1jhh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jhh, resolution 2.1&Aring;" /> '''LEXA S119A MUTANT'''<...)
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[[Image:1jhh.jpg|left|200px]]<br /><applet load="1jhh" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jhh.jpg|left|200px]]<br /><applet load="1jhh" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jhh, resolution 2.1&Aring;" />
caption="1jhh, resolution 2.1&Aring;" />
'''LEXA S119A MUTANT'''<br />
'''LEXA S119A MUTANT'''<br />
==Overview==
==Overview==
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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.
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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==
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1JHH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JHH OCA].
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1JHH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1JHH OCA].
==Reference==
==Reference==
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[[Category: Repressor lexA]]
[[Category: Repressor lexA]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Little, J.W.]]
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[[Category: Little, J W.]]
[[Category: Luo, Y.]]
[[Category: Luo, Y.]]
[[Category: Mosimann, S.]]
[[Category: Mosimann, S.]]
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[[Category: Pfuetzner, R.A.]]
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[[Category: Pfuetzner, R A.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: Strynadka, N C.J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: lexa sos repressor]]
[[Category: lexa sos repressor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:15:47 2007''
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''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


1jhh, resolution 2.1Å

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LEXA S119A 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

1JHH is a Single protein structure of sequence from Escherichia coli with as ligand. 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

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