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spinqualitylabelsall models 1thn, resolution 2.5Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structures of the ADP and ATP bound forms of the Bacillus Anti-sigma factor SpoIIAB in complex with the Anti-anti-sigma SpoIIAA: inhibitory complex with ADP, crystal form I

Overview

Cell type-specific transcription during Bacillus sporulation is, established by sigma(F), the activity of which is controlled by a, regulatory circuit involving the anti-sigma factor and serine kinase, SpoIIAB, and the anti-anti-sigma SpoIIAA. When ATP is present in the, nucleotide-binding site of SpoIIAB, SpoIIAA is phosphorylated, followed by, dissociation. The nucleotide-binding site of SpoIIAB is left bound to ADP., SpoIIAB(ADP) can bind an unphosphorylated molecule of SpoIIAA as a stable, binding partner. Thus, in this circuit, SpoIIAA plays a dual role as a, substrate of the SpoIIAB kinase activity, as well as a tight binding, inhibitor. Crystal structures of both the pre-phosphorylation complex and, the inhibitory complex, SpoIIAB(ATP) and SpoIIAB(ADP) bound to SpoIIAA, respectively, have been determined. The structural differences between the, two forms are subtle and confined to interactions with the phosphoryl, groups of the nucleotides. The structures reveal details of the, SpoIIAA:SpoIIAB interactions and how phosphorylated SpoIIAA dissociates, from SpoIIAB(ADP). Finally, the results confirm and expand upon the, docking model for SpoIIAA function as an anti-anti-sigma in releasing, sigma(F) from SpoIIAB.

About this Structure

1THN is a Protein complex structure of sequences from Geobacillus stearothermophilus with ADP and DMF as ligands. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Crystal structures of the ADP and ATP bound forms of the Bacillus anti-sigma factor SpoIIAB in complex with the anti-anti-sigma SpoIIAA., Masuda S, Murakami KS, Wang S, Anders Olson C, Donigian J, Leon F, Darst SA, Campbell EA, J Mol Biol. 2004 Jul 23;340(5):941-56. PMID:15236958

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