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New page: left|200px<br /><applet load="1djm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1djm" /> '''SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FR...
 
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[[Image:1djm.jpg|left|200px]]<br /><applet load="1djm" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1djm.jpg|left|200px]]<br /><applet load="1djm" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1djm" />
caption="1djm" />
'''SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI'''<br />
'''SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI'''<br />


==Overview==
==Overview==
The CheY protein is the response regulator in bacterial chemotaxis., Phosphorylation of a conserved aspartyl residue induces structural changes, that convert the protein from an inactive to an active state. The short, half-life of the aspartyl-phosphate has precluded detailed structural, analysis of the active protein. Persistent activation of Escherichia coli, CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the, structure determined by NMR spectroscopy to a backbone r.m.s.d. of, 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group, and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a, coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The, coupled rearrangement may be a more general mechanism for activation of, receiver domains.
The CheY protein is the response regulator in bacterial chemotaxis. Phosphorylation of a conserved aspartyl residue induces structural changes that convert the protein from an inactive to an active state. The short half-life of the aspartyl-phosphate has precluded detailed structural analysis of the active protein. Persistent activation of Escherichia coli CheY was achieved by complexation with beryllofluoride (BeF(3)(-)) and the structure determined by NMR spectroscopy to a backbone r.m.s.d. of 0.58(+/-0.08) A. Formation of a hydrogen bond between the Thr87 OH group and an active site acceptor, presumably Asp57.BeF(3)(-), stabilizes a coupled rearrangement of highly conserved residues, Thr87 and Tyr106, along with displacement of beta4 and H4, to yield the active state. The coupled rearrangement may be a more general mechanism for activation of receiver domains.


==About this Structure==
==About this Structure==
1DJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DJM OCA].  
1DJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DJM OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cho, H.S.]]
[[Category: Cho, H S.]]
[[Category: Kustu, S.]]
[[Category: Kustu, S.]]
[[Category: Lee, S.Y.]]
[[Category: Lee, S Y.]]
[[Category: Pan, X.]]
[[Category: Pan, X.]]
[[Category: Parkinson, J.S.]]
[[Category: Parkinson, J S.]]
[[Category: Pelton, J.G.]]
[[Category: Pelton, J G.]]
[[Category: Wemmer, D.E.]]
[[Category: Wemmer, D E.]]
[[Category: Yan, D.]]
[[Category: Yan, D.]]
[[Category: befx]]
[[Category: befx]]
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[[Category: two-component]]
[[Category: two-component]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:20:07 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:17:13 2008''