1buz
From Proteopedia
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==SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS NMR, MINIMIZED AVERAGE STRUCTURE== | ==SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS NMR, MINIMIZED AVERAGE STRUCTURE== | ||
| - | <StructureSection load='1buz' size='340' side='right' caption='[[1buz | + | <StructureSection load='1buz' size='340' side='right'caption='[[1buz]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1buz]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1buz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1buz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buz OCA], [https://pdbe.org/1buz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1buz RCSB], [https://www.ebi.ac.uk/pdbsum/1buz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1buz ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/SP2AA_BACSU SP2AA_BACSU] In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.<ref>PMID:8358793</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1buz_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1buz_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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=1buz ConSurf]. | </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=1buz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The establishment of differential gene expression in sporulating Bacillus subtilis involves four protein components, one of which, SpoIIAA, undergoes phosphorylation and dephosphorylation. We have used NMR spectroscopy to determine the solution structure of the nonphosphorylated form of SpoIIAA. The structure shows a fold consisting of a four-stranded beta-sheet and four alpha-helices. Knowledge of the structure helps to account for the phenotype of several strains of B. subtilis that carry known spoIIAA mutations and should facilitate investigations of the conformational consequences of phosphorylation. | ||
| - | + | ==See Also== | |
| - | + | *[[Anti-sigma factor antagonist 3D structures|Anti-sigma factor antagonist 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Campbell | + | [[Category: Large Structures]] |
| - | [[Category: Comfort | + | [[Category: Campbell ID]] |
| - | [[Category: Kovacs | + | [[Category: Comfort D]] |
| - | [[Category: Lord | + | [[Category: Kovacs H]] |
| - | [[Category: Yudkin | + | [[Category: Lord M]] |
| - | + | [[Category: Yudkin MD]] | |
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Current revision
SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS NMR, MINIMIZED AVERAGE STRUCTURE
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