1AUZ

SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS, NMR, 24 STRUCTURES

Summary for 1AUZ

Entry DOI	10.2210/pdb1auz/pdb
Descriptor	SPOIIAA (1 entity in total)
Functional Keywords	transcription regulator, kinase substrate, anti-anti sigma factor, novel alpha/beta fold
Biological source	Bacillus subtilis
Total number of polymer chains	1
Total formula weight	12874.98
Authors	Kovacs, H.,Comfort, D.,Lord, M.,Campbell, I.D.,Yudkin, M.D. (deposition date: 1997-09-08, release date: 1998-07-01, Last modification date: 2024-04-10)
Primary citation	Kovacs, H.,Comfort, D.,Lord, M.,Campbell, I.D.,Yudkin, M.D. Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis. Proc.Natl.Acad.Sci.USA, 95:5067-5071, 1998 Cited by PubMed Abstract: The establishment of differential gene expression in sporulating Bacillus subtilis involves four protein components, one of which, SpoIIAA, undergoes phosphorylation and dephosphorylation. We have used NMR spectroscopy to determine the solution structure of the nonphosphorylated form of SpoIIAA. The structure shows a fold consisting of a four-stranded beta-sheet and four alpha-helices. Knowledge of the structure helps to account for the phenotype of several strains of B. subtilis that carry known spoIIAA mutations and should facilitate investigations of the conformational consequences of phosphorylation. PubMed: 9560229 DOI: 10.1073/pnas.95.9.5067 PDB entries with the same primary citation
Experimental method	SOLUTION NMR

Structure validation