1qmp
From Proteopedia
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|PDB= 1qmp |SIZE=350|CAPTION= <scene name='initialview01'>1qmp</scene>, resolution 2.0Å | |PDB= 1qmp |SIZE=350|CAPTION= <scene name='initialview01'>1qmp</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmp OCA], [http://www.ebi.ac.uk/pdbsum/1qmp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qmp RCSB]</span> | ||
}} | }} | ||
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[[Category: Muchova, K.]] | [[Category: Muchova, K.]] | ||
[[Category: Wilkinson, A J.]] | [[Category: Wilkinson, A J.]] | ||
| - | [[Category: CA]] | ||
[[Category: response regulator]] | [[Category: response regulator]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:59 2008'' |
Revision as of 20:16, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHORYLATED ASPARTATE IN THE CRYSTAL STRUCTURE OF THE SPORULATION RESPONSE REGULATOR, SPO0A
Overview
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.
About this Structure
1QMP is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
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
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