1l0o
From Proteopedia
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Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF
Overview
Cell type-specific transcription during Bacillus sporulation is, established by sigmaF. SpoIIAB is an anti-sigma that binds and negatively, regulates sigmaF, as well as a serine kinase that phosphorylates and, inactivates the anti-anti-sigma SpoIIAA. The crystal structure of sigmaF, bound to the SpoIIAB dimer in the low-affinity, ADP form has been, determined at 2.9 A resolution. SpoIIAB adopts the GHKL superfamily fold, of ATPases and histidine kinases. A domain of sigmaF contacts both SpoIIAB, monomers, while 80% of the sigma factor is disordered. The interaction, occludes an RNA polymerase binding surface of sigmaF, explaining the, SpoIIAB anti-sigma activity. The structure also explains the specificity, of SpoIIAB for its target sigma factors and, in combination with genetic, and biochemical data, provides insight into the mechanism of SpoIIAA, anti-anti-sigma activity.
About this Structure
1L0O is a Protein complex structure of sequences from Geobacillus stearothermophilus with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF., Campbell EA, Masuda S, Sun JL, Muzzin O, Olson CA, Wang S, Darst SA, Cell. 2002 Mar 22;108(6):795-807. PMID:11955433
Page seeded by OCA on Tue Nov 20 20:08:36 2007
