1h4y | pdb_00001h4y

STRUCTURE OF THE ANTI-SIGMA FACTOR ANTAGONIST SPOIIAA IN ITS UNPHOSPHORYLATED FORM

spinqualitylabelsall models 1h4y, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h4y is a 2 chain structure with sequence from Lysinibacillus sphaericus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1h4x, 1h4z Resources: FirstGlance, OCA, RCSB, PDBsum 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 PubMed BACKGROUND: The asymmetric cell division during sporulation in Bacillus subtilis gives rise to two compartments: the mother cell and the forespore. Each follow different programs of gene expression coordinated by a succession of alternate RNA polymerase sigma factors. The activity of the first of these sigma factors, sigmaF, is restricted to the forespore although sigmaF is present in the predivisional cell and partitions into both compartments following the asymmetric septation. For sigmaF to become active, it must escape from a complex with its cognate anti-sigma factor, SpoIIAB. This relief from SpoIIAB inhibition requires the dephosphorylation of the anti-sigma factor antagonist, SpoIIAA. The phosphorylation state of SpoIIAA is thus a key determinant of sigmaF activity and cell fate. RESULTS: We have solved the crystal structures of SpoIIAA from Bacillus sphaericus in its phosphorylated and unphosphorylated forms. The overall structure consists of a central beta-pleated sheet, one face of which is buried by a pair of alpha helices, while the other is largely exposed to solvent. The site of phosphorylation, Ser57, is located at the N terminus of helix alpha2. The phosphoserine is exceptionally well defined in the 1.2 A electron density maps, revealing that the structural changes accompanying phosphorylation are slight. CONCLUSIONS: Comparison of unphosphorylated and phosphorylated SpoIIAA shows that covalent modification has no significant effect on the global structure of the protein. The phosphoryl group has a passive role as a negatively charged flag rather than the active role it plays as a nucleus of structural reorganization in many eukaryotic signaling systems. Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms.,Seavers PR, Lewis RJ, Brannigan JA, Verschueren KH, Murshudov GN, Wilkinson AJ Structure. 2001 Jul 3;9(7):605-14. PMID:11470435 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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