1a0o

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(New page: 200px<br /><applet load="1a0o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a0o, resolution 2.95&Aring;" /> '''CHEY-BINDING DOMAIN ...)
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[[Image:1a0o.gif|left|200px]]<br /><applet load="1a0o" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a0o.gif|left|200px]]<br /><applet load="1a0o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a0o, resolution 2.95&Aring;" />
caption="1a0o, resolution 2.95&Aring;" />
'''CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY'''<br />
'''CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY'''<br />
==Overview==
==Overview==
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Bacterial adaptation to the environment is accomplished through the, coordinated activation of specific sensory receptors and signal processing, proteins. Among the best characterized of these pathways are those which, employ the two-component paradigm. In these systems, signal transmission, is mediated by Mg(2+)-dependent phospho-relay reactions between histidine, auto-kinases and phospho-accepting receiver domains in response-regulator, proteins. Although this mechanism of activation is common to all, response-regulators, detrimental cross-talk between different, two-component pathways within the same cell is minimized through the use, of specific recognition domains. Here, we report the crystal structure, at, 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low, affinity complex (KD = 2 microM), may also contribute to the mechanism of, CheY activation.
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Bacterial adaptation to the environment is accomplished through the coordinated activation of specific sensory receptors and signal processing proteins. Among the best characterized of these pathways are those which employ the two-component paradigm. In these systems, signal transmission is mediated by Mg(2+)-dependent phospho-relay reactions between histidine auto-kinases and phospho-accepting receiver domains in response-regulator proteins. Although this mechanism of activation is common to all response-regulators, detrimental cross-talk between different two-component pathways within the same cell is minimized through the use of specific recognition domains. Here, we report the crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low affinity complex (KD = 2 microM), may also contribute to the mechanism of CheY activation.
==About this Structure==
==About this Structure==
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1A0O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A0O OCA].
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1A0O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A0O OCA].
==Reference==
==Reference==
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[[Category: Chinardet, N.]]
[[Category: Chinardet, N.]]
[[Category: Mourey, L.]]
[[Category: Mourey, L.]]
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[[Category: Samama, J.P.]]
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[[Category: Samama, J P.]]
[[Category: Welch, M.]]
[[Category: Welch, M.]]
[[Category: MN]]
[[Category: MN]]
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[[Category: two-component system]]
[[Category: two-component system]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:32:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:40 2008''

Revision as of 09:39, 21 February 2008


1a0o, resolution 2.95Å

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CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY

Overview

Bacterial adaptation to the environment is accomplished through the coordinated activation of specific sensory receptors and signal processing proteins. Among the best characterized of these pathways are those which employ the two-component paradigm. In these systems, signal transmission is mediated by Mg(2+)-dependent phospho-relay reactions between histidine auto-kinases and phospho-accepting receiver domains in response-regulator proteins. Although this mechanism of activation is common to all response-regulators, detrimental cross-talk between different two-component pathways within the same cell is minimized through the use of specific recognition domains. Here, we report the crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low affinity complex (KD = 2 microM), may also contribute to the mechanism of CheY activation.

About this Structure

1A0O is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY., Welch M, Chinardet N, Mourey L, Birck C, Samama JP, Nat Struct Biol. 1998 Jan;5(1):25-9. PMID:9437425

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