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1p6q

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{{STRUCTURE_1p6q| PDB=1p6q | SCENE= }}
{{STRUCTURE_1p6q| PDB=1p6q | SCENE= }}
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'''NMR Structure of the Response regulator CheY2 from Sinorhizobium meliloti, complexed with Mg++'''
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===NMR Structure of the Response regulator CheY2 from Sinorhizobium meliloti, complexed with Mg++===
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==Overview==
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The chemotactic signalling chain to the flagellar motor of Sinorhizobium meliloti features a new type of response regulator, CheY2. CheY2 activated by phosphorylation (CheY2-P) controls the rotary speed of the flagellar motor (instead of reversing the sense of rotation), and it is efficiently dephosphorylated by phospho-retrotransfer to the cognate kinase, CheA. Here, we report the NMR solution structures of the Mg(2+)-complex of inactive CheY2, and of activated CheY2-BeF(3), a stable analogue of CheY2-P, to an overall root mean square deviation of 0.042 nm and 0.027 nm, respectively. The 14 kDa CheY2 protein exhibits a characteristic open (alpha/beta)(5) conformation. Modification of CheY2 by BeF(3)(-) leads to large conformational changes of the protein, which are in the limits of error identical with those observed by phosphorylation of the active-centre residue Asp58. In BeF(3)-activated CheY2, the position of Thr88-OH favours the formation of a hydrogen bond with the active site, Asp58-BeF(3), similar to BeF(3)-activated CheY from Escherichia coli. In contrast to E.coli, this reorientation is not involved in a Tyr-Thr-coupling mechanism, that propagates the signal from the incoming phosphoryl group to the C-terminally located FliM-binding surface. Rather, a rearrangement of the Phe59 side-chain to interact with Ile86-Leu95-Val96 along with a displacement of alpha4 towards beta5 is stabilised in S.meliloti. The resulting, activation-induced, compact alpha4-beta5-alpha5 surface forms a unique binding domain suited for specific interaction with and signalling to a rotary motor that requires a gradual speed control. We propose that these new features of response regulator activation, compared to other two-component systems, are the key for the observed unique phosphorylation, dephosphorylation and motor control mechanisms in S.meliloti.
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{{ABSTRACT_PUBMED_15066432}}
==About this Structure==
==About this Structure==
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1P6Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6Q OCA].
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1P6Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6Q OCA].
==Reference==
==Reference==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:09:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:05:23 2008''

Revision as of 23:05, 27 July 2008

Image:1p6q.png

Template:STRUCTURE 1p6q

NMR Structure of the Response regulator CheY2 from Sinorhizobium meliloti, complexed with Mg++

Template:ABSTRACT PUBMED 15066432

About this Structure

1P6Q is a Single protein structure of sequence from Sinorhizobium meliloti. Full experimental information is available from OCA.

Reference

Solution structures of the inactive and BeF3-activated response regulator CheY2., Riepl H, Scharf B, Schmitt R, Kalbitzer HR, Maurer T, J Mol Biol. 2004 Apr 23;338(2):287-97. PMID:15066432

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