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3fyr

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Revision as of 06:52, 1 November 2017

Crystal structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis

Structural highlights

3fyr is a 3 chain structure with sequence from Bacsu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	BSU25690, sda (BACSU)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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

The crystal structure of the DNA-damage checkpoint inhibitor of sporulation, Sda, from Bacillus subtilis, has been solved by the MAD technique using selenomethionine-substituted protein. The structure closely resembles that previously solved by NMR, as well as the structure of a homologue from Geobacillus stearothermophilus solved in complex with the histidine kinase KinB. The structure contains three molecules in the asymmetric unit. The unusual trimeric arrangement, which lacks simple internal symmetry, appears to be preserved in solution based on an essentially ideal fit to previously acquired scattering data for Sda in solution. This interpretation contradicts previous findings that Sda was monomeric or dimeric in solution. This study demonstrates the difficulties that can be associated with the characterization of small proteins and the value of combining multiple biophysical techniques. It also emphasizes the importance of understanding the physical principles behind these techniques and therefore their limitations.

Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state.,Jacques DA, Streamer M, Rowland SL, King GF, Guss JM, Trewhella J, Langley DB Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):574-81. Epub 2009, May 15. PMID:19465772^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Burkholder WF, Kurtser I, Grossman AD. Replication initiation proteins regulate a developmental checkpoint in Bacillus subtilis. Cell. 2001 Jan 26;104(2):269-79. PMID:11207367
↑ Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF. Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis. Mol Cell. 2004 Mar 12;13(5):689-701. PMID:15023339
↑ Jacques DA, Streamer M, Rowland SL, King GF, Guss JM, Trewhella J, Langley DB. Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallogr D Biol Crystallogr. 2009 Jun;65(Pt 6):574-81. Epub 2009, May 15. PMID:19465772 doi:10.1107/S090744490901169X

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fyr"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis==
 <StructureSection load='3fyr' size='340' side='right' caption='[[3fyr]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU25690, sda ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyr OCA], [http://pdbe.org/3fyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fyr RCSB], [http://www.ebi.ac.uk/pdbsum/3fyr PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fyr OCA], [http://pdbe.org/3fyr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fyr RCSB], [http://www.ebi.ac.uk/pdbsum/3fyr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fyr ProSAT]</span></td></tr>
 </table>
 == Function ==

3fyr

From Proteopedia

Revision as of 06:52, 1 November 2017

Crystal structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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