1h4x

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[[Image:1h4x.gif|left|200px]]
 
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==Structure of the Bacillus Cell Fate Determinant SpoIIAA in the Phosphorylated Form==
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The line below this paragraph, containing "STRUCTURE_1h4x", creates the "Structure Box" on the page.
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<StructureSection load='1h4x' size='340' side='right'caption='[[1h4x]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1h4x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4X FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.16&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_1h4x| PDB=1h4x | SCENE= }}
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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=1h4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4x OCA], [https://pdbe.org/1h4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4x RCSB], [https://www.ebi.ac.uk/pdbsum/1h4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SP2AA_LYSSH SP2AA_LYSSH] In the phosphorylated form it could act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma f from inhibition.
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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/h4/1h4x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1h4x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: The asymmetric cell division during sporulation in Bacillus subtilis gives rise to two compartments: the mother cell and the forespore. Each follow different programs of gene expression coordinated by a succession of alternate RNA polymerase sigma factors. The activity of the first of these sigma factors, sigmaF, is restricted to the forespore although sigmaF is present in the predivisional cell and partitions into both compartments following the asymmetric septation. For sigmaF to become active, it must escape from a complex with its cognate anti-sigma factor, SpoIIAB. This relief from SpoIIAB inhibition requires the dephosphorylation of the anti-sigma factor antagonist, SpoIIAA. The phosphorylation state of SpoIIAA is thus a key determinant of sigmaF activity and cell fate. RESULTS: We have solved the crystal structures of SpoIIAA from Bacillus sphaericus in its phosphorylated and unphosphorylated forms. The overall structure consists of a central beta-pleated sheet, one face of which is buried by a pair of alpha helices, while the other is largely exposed to solvent. The site of phosphorylation, Ser57, is located at the N terminus of helix alpha2. The phosphoserine is exceptionally well defined in the 1.2 A electron density maps, revealing that the structural changes accompanying phosphorylation are slight. CONCLUSIONS: Comparison of unphosphorylated and phosphorylated SpoIIAA shows that covalent modification has no significant effect on the global structure of the protein. The phosphoryl group has a passive role as a negatively charged flag rather than the active role it plays as a nucleus of structural reorganization in many eukaryotic signaling systems.
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'''STRUCTURE OF THE BACILLUS CELL FATE DETERMINANT SPOIIAA IN THE PHOSPHORYLATED FORM'''
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Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms.,Seavers PR, Lewis RJ, Brannigan JA, Verschueren KH, Murshudov GN, Wilkinson AJ Structure. 2001 Jul 3;9(7):605-14. PMID:11470435<ref>PMID:11470435</ref>
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==Overview==
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BACKGROUND: The asymmetric cell division during sporulation in Bacillus subtilis gives rise to two compartments: the mother cell and the forespore. Each follow different programs of gene expression coordinated by a succession of alternate RNA polymerase sigma factors. The activity of the first of these sigma factors, sigmaF, is restricted to the forespore although sigmaF is present in the predivisional cell and partitions into both compartments following the asymmetric septation. For sigmaF to become active, it must escape from a complex with its cognate anti-sigma factor, SpoIIAB. This relief from SpoIIAB inhibition requires the dephosphorylation of the anti-sigma factor antagonist, SpoIIAA. The phosphorylation state of SpoIIAA is thus a key determinant of sigmaF activity and cell fate. RESULTS: We have solved the crystal structures of SpoIIAA from Bacillus sphaericus in its phosphorylated and unphosphorylated forms. The overall structure consists of a central beta-pleated sheet, one face of which is buried by a pair of alpha helices, while the other is largely exposed to solvent. The site of phosphorylation, Ser57, is located at the N terminus of helix alpha2. The phosphoserine is exceptionally well defined in the 1.2 A electron density maps, revealing that the structural changes accompanying phosphorylation are slight. CONCLUSIONS: Comparison of unphosphorylated and phosphorylated SpoIIAA shows that covalent modification has no significant effect on the global structure of the protein. The phosphoryl group has a passive role as a negatively charged flag rather than the active role it plays as a nucleus of structural reorganization in many eukaryotic signaling systems.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1H4X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lysinibacillus_sphaericus Lysinibacillus sphaericus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4X OCA].
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</div>
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<div class="pdbe-citations 1h4x" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms., Seavers PR, Lewis RJ, Brannigan JA, Verschueren KH, Murshudov GN, Wilkinson AJ, Structure. 2001 Jul 3;9(7):605-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11470435 11470435]
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*[[Anti-sigma factor antagonist 3D structures|Anti-sigma factor antagonist 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Lysinibacillus sphaericus]]
[[Category: Lysinibacillus sphaericus]]
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[[Category: Single protein]]
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[[Category: Brannigan JA]]
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[[Category: Brannigan, J A.]]
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[[Category: Lewis RJ]]
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[[Category: Lewis, R J.]]
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[[Category: Murshudov GN]]
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[[Category: Murshudov, G N.]]
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[[Category: Seavers PR]]
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[[Category: Seavers, P R.]]
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[[Category: Verschueren KHG]]
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[[Category: Verschueren, K H.G.]]
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[[Category: Wilkinson AJ]]
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[[Category: Wilkinson, A J.]]
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[[Category: Cell differentiation]]
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[[Category: Crystallography]]
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[[Category: Phosphorylation]]
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[[Category: Sigma factor]]
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[[Category: Sporulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:26:06 2008''
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Current revision

Structure of the Bacillus Cell Fate Determinant SpoIIAA in the Phosphorylated Form

PDB ID 1h4x

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