1ixm
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(New page: 200px<br /><applet load="1ixm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ixm, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 15:37, 20 November 2007
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CRYSTAL STRUCTURE OF SPOOB FROM BACILLUS SUBTILIS
Overview
A basis for understanding specificity of molecular recognition between, phosphorelay proteins has been deduced from the 2.6 A structure of the, Spo0B phosphotransferase of the phosphorelay regulating sporulation, initiation. Spo0B consists of two domains: an N-terminal alpha-helical, hairpin domain and a C-terminal alpha/beta domain. Two subunits of Spo0B, dimerize by a parallel association of helical hairpins to form a novel, four-helix bundle from which the active histidine protrudes. Docking, studies show that both the monomers interact with a Spo0F molecule at the, region surrounding the active site aspartate to position it for, phosphotransfer. It is apparent that different surfaces of response, regulators may be involved in recognition of the protein partners to which, they are paired.
About this Structure
1IXM is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase., Varughese KI, Madhusudan, Zhou XZ, Whiteley JM, Hoch JA, Mol Cell. 1998 Oct;2(4):485-93. PMID:9809070
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