1p6q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p6q.jpg|left|200px]]<br /><applet load="1p6q" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1p6q.jpg|left|200px]]
-
caption="1p6q" />
+
 
-
'''NMR Structure of the Response regulator CheY2 from Sinorhizobium meliloti, complexed with Mg++'''<br />
+
{{Structure
 +
|PDB= 1p6q |SIZE=350|CAPTION= <scene name='initialview01'>1p6q</scene>
 +
|SITE=
 +
|LIGAND=
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''NMR Structure of the Response regulator CheY2 from Sinorhizobium meliloti, complexed with Mg++'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1P6Q is a [http://en.wikipedia.org/wiki/Single_protein 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].
+
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].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15066432 15066432]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/15066432 15066432]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sinorhizobium meliloti]]
[[Category: Sinorhizobium meliloti]]
Line 25: Line 34:
[[Category: sinorhizobium meliloti]]
[[Category: sinorhizobium meliloti]]
[[Category: spine]]
[[Category: spine]]
-
[[Category: structural genomics]]
+
[[Category: structural genomic]]
[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:42 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:20:37 2008''

Revision as of 11:20, 20 March 2008


PDB ID 1p6q

Drag the structure with the mouse to rotate
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1P6Q is a Single protein structure of sequence from Sinorhizobium meliloti. Full crystallographic 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

Page seeded by OCA on Thu Mar 20 13:20:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools