1L0O

Crystal Structure of the Bacillus stearothermophilus Anti-Sigma Factor SpoIIAB with the Sporulation Sigma Factor SigmaF

Summary for 1L0O

• Entry DOI: 10.2210/pdb1l0o/pdb
• Descriptor: Anti-sigma F factor, sigma factor, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: bergerat fold, helix-turn-helix, protein binding
• Biological source: Geobacillus stearothermophilus; More
• Total number of polymer chains: 3
• Total formula weight: 62374.72

Authors

Campbell, E.A.,Masuda, S.,Sun, J.L.,Muzzin, O.,Olson, C.A.,Wang, S.,Darst, S.A. (deposition date: 2002-02-12, release date: 2002-04-03, Last modification date: 2024-02-14)

Primary citation

Campbell, E.A.,Masuda, S.,Sun, J.L.,Muzzin, O.,Olson, C.A.,Wang, S.,Darst, S.A.
Crystal structure of the Bacillus stearothermophilus anti-sigma factor SpoIIAB with the sporulation sigma factor sigmaF.
Cell(Cambridge,Mass.), 108:795-807, 2002

PubMed Abstract: 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.

PubMed: 11955433
DOI: 10.1016/S0092-8674(02)00662-1

Experimental method

X-RAY DIFFRACTION (2.9 Å)