1qmp | pdb_00001qmp

Phosphorylated aspartate in the crystal structure of the sporulation response regulator, Spo0A

spinqualitylabelsall models 1qmp, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qmp is a 4 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA NonStd Res: PHD Gene: spo0A (ATCC 12980) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SP0A_GEOSE] May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with Spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process. Repressor of abrB, activator of the spoIIa operon. Binds the DNA sequence 5'-TGNCGAA-3' (0A box) (By similarity). 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 Phosphorylation of aspartic acid residues is the hallmark of two- component signal transduction systems that orchestrate the adaptive responses of micro-organisms to changes in their surroundings. Two-component systems consist of a sensor kinase that interprets environmental signals and a response regulator that activates the appropriate physiological response. Although structures of response regulators are known, little is understood about their activated phosphorylated forms, due to the intrinsic instability of the acid phosphate linkage. Here, we report the phosphorylated structure of the receiver/phosphoacceptor domain of Spo0A, the master regulator of sporulation, from Bacillus stearothermophilus. The phosphoryl group is covalently bonded to the invariant aspartate 55, and co-ordinated to a nearby divalent metal cation, with both species fulfilling their electrostatic potential through interactions with solvent water molecules, the protein main chain, and with side-chains of amino acid residues strongly conserved across the response regulator family. This is the first direct visualisation of a phosphoryl group covalently linked to an aspartic acid residue in any protein, with implications for signalling within the response regulator family. Phosphorylated aspartate in the structure of a response regulator protein.,Lewis RJ, Brannigan JA, Muchova K, Barak I, Wilkinson AJ J Mol Biol. 1999 Nov 19;294(1):9-15. PMID:10556024 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Response regulator 3D structure

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