3d36
From Proteopedia
(Difference between revisions)
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<StructureSection load='3d36' size='340' side='right'caption='[[3d36]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='3d36' size='340' side='right'caption='[[3d36]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3d36]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3d36]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus_10 Geobacillus stearothermophilus 10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D36 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">X-ray diffraction, [[Resolution|Resolution]] 2.03Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
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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=3d36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d36 OCA], [https://pdbe.org/3d36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d36 RCSB], [https://www.ebi.ac.uk/pdbsum/3d36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d36 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=3d36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d36 OCA], [https://pdbe.org/3d36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d36 RCSB], [https://www.ebi.ac.uk/pdbsum/3d36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d36 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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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=3d36 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=3d36 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Entry to sporulation in bacilli is governed by a histidine kinase phosphorelay, a variation of the predominant signal transduction mechanism in prokaryotes. Sda directly inhibits sporulation histidine kinases in response to DNA damage and replication defects. We determined a 2.0-A-resolution X-ray crystal structure of the intact cytoplasmic catalytic core [comprising the dimerization and histidine phosphotransfer domain (DHp domain), connected to the ATP binding catalytic domain] of the Geobacillus stearothermophilus sporulation kinase KinB complexed with Sda. Structural and biochemical analyses reveal that Sda binds to the base of the DHp domain and prevents molecular transactions with the DHp domain to which it is bound by acting as a simple molecular barricade. Sda acts to sterically block communication between the catalytic domain and the DHp domain, which is required for autophosphorylation, as well as to sterically block communication between the response regulator Spo0F and the DHp domain, which is required for phosphotransfer and phosphatase activities. | ||
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- | How to Switch Off a Histidine Kinase: Crystal Structure of Geobacillus stearothermophilus KinB with the inhibitor Sda.,Bick MJ, Lamour V, Rajashankar KR, Gordiyenko Y, Robinson CV, Darst SA J Mol Biol. 2008 Dec 11. PMID:19101565<ref>PMID:19101565</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3d36" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Geobacillus stearothermophilus 10]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Bick | + | [[Category: Bick MJ]] |
- | [[Category: Darst | + | [[Category: Darst SA]] |
- | [[Category: Gordiyenko | + | [[Category: Gordiyenko Y]] |
- | [[Category: Lamour | + | [[Category: Lamour V]] |
- | [[Category: Rajashankar | + | [[Category: Rajashankar KR]] |
- | [[Category: Robinson | + | [[Category: Robinson CV]] |
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Current revision
How to Switch Off a Histidine Kinase: Crystal Structure of Geobacillus stearothermophilus KinB with the Inhibitor Sda
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