1buz | pdb_00001buz
From Proteopedia
SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS NMR, MINIMIZED AVERAGE STRUCTURE
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Structural highlights
Function[SP2AA_BACSU] In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.[1] 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 PubMedThe 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. Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis.,Kovacs H, Comfort D, Lord M, Campbell ID, Yudkin MD Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):5067-71. PMID:9560229[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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