1ixm

From Proteopedia

CRYSTAL STRUCTURE OF SPOOB FROM BACILLUS SUBTILIS

PDB ID 1ixm

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Structural highlights

1ixm is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SP0B_BACSU Key element in the phosphorelay regulating sporulation initiation. Acts on spo0A. Mediates reversible phosphoryl transfer from spo0F to spo0A.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Varughese KI, Madhusudan, Zhou XZ, Whiteley JM, Hoch JA. Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase. Mol Cell. 1998 Oct;2(4):485-93. PMID:9809070