1pv0
From Proteopedia
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==Structure of the Sda antikinase== | ==Structure of the Sda antikinase== | ||
| - | <StructureSection load='1pv0' size='340' side='right'caption='[[1pv0 | + | <StructureSection load='1pv0' size='340' side='right'caption='[[1pv0]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1pv0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1pv0]] 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=1PV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PV0 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'>[https://proteopedia.org/fgij/fg.htm?mol=1pv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pv0 OCA], [https://pdbe.org/1pv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1pv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pv0 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=1pv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pv0 OCA], [https://pdbe.org/1pv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pv0 RCSB], [https://www.ebi.ac.uk/pdbsum/1pv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pv0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SDA_BACSU SDA_BACSU] Mediates a developmental checkpoint inhibiting initiation of sporulation (by preventing phosphorylation of spo0A) in response to defects in the replication initiation machinery. Inhibits autophosphorylation of the histidine protein kinase KinA, forming a molecular barricade that prevents productive interaction between the ATP-binding site in the catalytic domain and the phosphorylatable His in the phosphotransfer domain of KinA. Probably also inhibits the activity of KinB, but has relatively little effect on KinC. Has at least one target in vivo in addition to KinA as sda does not require KinA to inhibit sporulation.<ref>PMID:11207367</ref> <ref>PMID:15023339</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1pv0 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=1pv0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Histidine kinases are used extensively in prokaryotes to monitor and respond to changes in cellular and environmental conditions. In Bacillus subtilis, sporulation-specific gene expression is controlled by a histidine kinase phosphorelay that culminates in phosphorylation of the Spo0A transcription factor. Sda provides a developmental checkpoint by inhibiting this phosphorelay in response to DNA damage and replication defects. We show that Sda acts at the first step in the relay by inhibiting autophosphorylation of the histidine kinase KinA. The structure of Sda, which we determined using NMR, comprises a helical hairpin. A cluster of conserved residues on one face of the hairpin mediates an interaction between Sda and the KinA dimerization/phosphotransfer domain. This interaction stabilizes the KinA dimer, and the two proteins form a stable heterotetramer. The data indicate that Sda forms a molecular barricade that inhibits productive interaction between the catalytic and phosphotransfer domains of KinA. | ||
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| - | Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis.,Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF Mol Cell. 2004 Mar 12;13(5):689-701. PMID:15023339<ref>PMID:15023339</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1pv0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Burkholder | + | [[Category: Burkholder WF]] |
| - | [[Category: Grossman | + | [[Category: Grossman AD]] |
| - | [[Category: King | + | [[Category: King GF]] |
| - | [[Category: Maciejewski | + | [[Category: Maciejewski MW]] |
| - | [[Category: Rowland | + | [[Category: Rowland SL]] |
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Revision as of 05:59, 17 April 2024
Structure of the Sda antikinase
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