This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ixm
From Proteopedia
| |||||||
| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | SPO0B (Bacillus subtilis) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Sun Mar 30 21:26:08 2008
