1p6q

<StructureSection load='1p6q' size='340' side='right'caption='[[1p6q]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1p6q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_9930 Atcc 9930]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6Q FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p6u|1p6u]]</div></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15066432</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1p6q" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Atcc 9930]]

[[Category: Kalbitzer, H R]]

[[Category: Maurer, T]]

[[Category: Riepl, H]]

[[Category: SPINE, Structural Proteomics in Europe]]

[[Category: Scharf, B]]

[[Category: Schmitt, R]]

[[Category: Chemotaxis]]

[[Category: Chey2]]

[[Category: Response regulator]]

[[Category: Signal transduction]]

[[Category: Signaling protein]]

[[Category: Spine]]

[[Category: Structural genomic]]

[[Category: Structural proteomics in europe]]