1qmp

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[[Image:1qmp.jpg|left|200px]]
 
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{{Structure
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==Phosphorylated aspartate in the crystal structure of the sporulation response regulator, Spo0A==
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|PDB= 1qmp |SIZE=350|CAPTION= <scene name='initialview01'>1qmp</scene>, resolution 2.0&Aring;
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<StructureSection load='1qmp' size='340' side='right'caption='[[1qmp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene>
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<table><tr><td colspan='2'>[[1qmp]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QMP FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmp OCA], [https://pdbe.org/1qmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qmp RCSB], [https://www.ebi.ac.uk/pdbsum/1qmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qmp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|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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== Function ==
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}}
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[https://www.uniprot.org/uniprot/SP0A_GEOSE 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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qm/1qmp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qmp ConSurf].
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<div style="clear:both"></div>
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'''PHOSPHORYLATED ASPARTATE IN THE CRYSTAL STRUCTURE OF THE SPORULATION RESPONSE REGULATOR, SPO0A'''
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==See Also==
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*[[Response regulator 3D structure|Response regulator 3D structure]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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1QMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMP OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10556024 10556024]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Barak, I.]]
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[[Category: Barak I]]
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[[Category: Brannigan, J A.]]
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[[Category: Brannigan JA]]
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[[Category: Lewis, R J.]]
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[[Category: Lewis RJ]]
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[[Category: Muchova, K.]]
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[[Category: Muchova K]]
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[[Category: Wilkinson, A J.]]
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[[Category: Wilkinson AJ]]
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[[Category: response regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:59 2008''
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Current revision

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

PDB ID 1qmp

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