1jbe

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(New page: 200px<br /><applet load="1jbe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jbe, resolution 1.08&Aring;" /> '''1.08 A Structure of ...)
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[[Image:1jbe.jpg|left|200px]]<br /><applet load="1jbe" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jbe, resolution 1.08&Aring;" />
caption="1jbe, resolution 1.08&Aring;" />
'''1.08 A Structure of apo-Chey reveals meta-active conformation'''<br />
'''1.08 A Structure of apo-Chey reveals meta-active conformation'''<br />
==Overview==
==Overview==
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CheY is the best characterized member of the response regulator, superfamily, and as such it has become the principal model for, understanding the initial molecular mechanisms of signaling in, two-component systems. Normal signaling by response regulators requires, phosphorylation, in combination with an activation mechanism whose, conformational effects are not completely understood. CheY activation, involves three events, phosphorylation, a conformational change in the, beta(4)--alpha(4) loop, and a rotational restriction of the side chain of, tyrosine 106. An outstanding question concerns the nature of an active, conformation in the apoCheY population. The details of this 1.08-A, resolution crystal structure of wild-type apoCheY shows the, beta(4)--alpha(4) loop in two distinctly different conformations that, sterically correlate with the two rotameric positions of the tyrosine 106, side chain. One of these conformational states of CheY is the inactive, form, and we propose that the other is a meta-active form, responsible for, the active properties seen in apoCheY.
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CheY is the best characterized member of the response regulator superfamily, and as such it has become the principal model for understanding the initial molecular mechanisms of signaling in two-component systems. Normal signaling by response regulators requires phosphorylation, in combination with an activation mechanism whose conformational effects are not completely understood. CheY activation involves three events, phosphorylation, a conformational change in the beta(4)--alpha(4) loop, and a rotational restriction of the side chain of tyrosine 106. An outstanding question concerns the nature of an active conformation in the apoCheY population. The details of this 1.08-A resolution crystal structure of wild-type apoCheY shows the beta(4)--alpha(4) loop in two distinctly different conformations that sterically correlate with the two rotameric positions of the tyrosine 106 side chain. One of these conformational states of CheY is the inactive form, and we propose that the other is a meta-active form, responsible for the active properties seen in apoCheY.
==About this Structure==
==About this Structure==
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1JBE 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 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JBE OCA].
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1JBE 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> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBE OCA].
==Reference==
==Reference==
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[[Category: chey]]
[[Category: chey]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:04:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:46 2008''

Revision as of 11:20, 21 February 2008

Image:1jbe.jpg

1jbe, resolution 1.08Å

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1.08 A Structure of apo-Chey reveals meta-active conformation

Overview

CheY is the best characterized member of the response regulator superfamily, and as such it has become the principal model for understanding the initial molecular mechanisms of signaling in two-component systems. Normal signaling by response regulators requires phosphorylation, in combination with an activation mechanism whose conformational effects are not completely understood. CheY activation involves three events, phosphorylation, a conformational change in the beta(4)--alpha(4) loop, and a rotational restriction of the side chain of tyrosine 106. An outstanding question concerns the nature of an active conformation in the apoCheY population. The details of this 1.08-A resolution crystal structure of wild-type apoCheY shows the beta(4)--alpha(4) loop in two distinctly different conformations that sterically correlate with the two rotameric positions of the tyrosine 106 side chain. One of these conformational states of CheY is the inactive form, and we propose that the other is a meta-active form, responsible for the active properties seen in apoCheY.

About this Structure

1JBE is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY., Simonovic M, Volz K, J Biol Chem. 2001 Aug 3;276(31):28637-40. Epub 2001 Jun 15. PMID:11410584

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