1kmi
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1kmi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kmi, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...)
Next diff →
Revision as of 17:14, 20 November 2007
|
CRYSTAL STRUCTURE OF AN E.COLI CHEMOTAXIS PROTEIN, CHEZ
Overview
The protein CheZ, which has the last unknown structure in the Escherichia, coli chemotaxis pathway, stimulates the dephosphorylation of the response, regulator CheY by an unknown mechanism. Here we report the co-crystal, structure of CheZ with CheY, Mg(2+) and the phosphoryl analog, BeF(3)(-)., The predominant structural feature of the CheZ dimer is a long four-helix, bundle composed of two helices from each monomer. The side chain of Gln, 147 of CheZ inserts into the CheY active site and is essential to the, dephosphorylation activity of CheZ. Gln 147 may orient a water molecule, for nucleophilic attack, similar to the role of the conserved Gln residue, in the RAS family of GTPases. Similarities between the CheY[bond] CheZ and, Spo0F [bond]Spo0B structures suggest a general mode of interaction for, modulation of response regulator phosphorylation chemistry.
About this Structure
1KMI is a Protein complex structure of sequences from Escherichia coli with MG, BEF and BCN as ligands. Full crystallographic information is available from OCA.
Reference
Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ., Zhao R, Collins EJ, Bourret RB, Silversmith RE, Nat Struct Biol. 2002 Aug;9(8):570-5. PMID:12080332
Page seeded by OCA on Tue Nov 20 19:22:08 2007
