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| | <StructureSection load='1dz3' size='340' side='right'caption='[[1dz3]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='1dz3' size='340' side='right'caption='[[1dz3]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1dz3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DZ3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1DZ3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1dz3]] is a 1 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=1DZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZ3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spo0A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1dz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz3 OCA], [http://pdbe.org/1dz3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dz3 RCSB], [http://www.ebi.ac.uk/pdbsum/1dz3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz3 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dz3 OCA], [https://pdbe.org/1dz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dz3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dz3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 12980]] | + | [[Category: Geobacillus stearothermophilus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barak, I]] | + | [[Category: Barak I]] |
| - | [[Category: Brannigan, J A]] | + | [[Category: Brannigan JA]] |
| - | [[Category: Leonard, G]] | + | [[Category: Leonard G]] |
| - | [[Category: Lewis, R J]] | + | [[Category: Lewis RJ]] |
| - | [[Category: Muchova, K]] | + | [[Category: Muchova K]] |
| - | [[Category: Wilkinson, A J]] | + | [[Category: Wilkinson AJ]] |
| - | [[Category: Domain swapping]]
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| - | [[Category: Response regulator]]
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| Structural highlights
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
Adaptive responses of micro-organisms, such as chemotaxis and sporulation, are governed by two-component systems consisting of sensor kinases, that interpret environmental signals, and response regulators which activate the appropriate physiological responses. Signal transduction via response regulator proteins is mediated through transient phosphorylation of aspartic acid residues. In Spo0A, the key regulator of development (sporulation) in Bacillus, phosphorylation of the N-terminal receiver domain (N-Spo0A) at aspartate-55 switches on the transcription activation functions residing in the C-terminal effector domain. Here we report the crystal structure of N-Spo0A from Bacillus stearothermophilus at 1.6 A spacing, revealing a dimer formed by an alpha-helix swap. Comparison of this structure with the recently described structure of phosphorylated N-Spo0A shows that dimer formation results from a cis-trans isomerization of the Lys106--Pro107 peptide bond. The quaternary reorganization is associated with alterations in the active site stereochemistry which may have implications for signalling. Remarkably, this 3-D domain swapped N-Spo0A dimer has an identical topology to a hypothetical CheY-like dimer, recently proposed as an intermediate in the evolution of the family of periplasmic substrate binding proteins.
Domain swapping in the sporulation response regulator Spo0A.,Lewis RJ, Muchova K, Brannigan JA, Barak I, Leonard G, Wilkinson AJ J Mol Biol. 2000 Mar 31;297(3):757-70. PMID:10731426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lewis RJ, Muchova K, Brannigan JA, Barak I, Leonard G, Wilkinson AJ. Domain swapping in the sporulation response regulator Spo0A. J Mol Biol. 2000 Mar 31;297(3):757-70. PMID:10731426 doi:10.1006/jmbi.2000.3598
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