Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state

Jacques, D. A., Streamer, M, Rowland, S. L., King, G. F., Guss, J. M., Trewhella, J and Langley, D. B. (2009) Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state. Acta Crystallographica Section D: Biological Crystallography, 65 Part 6: 574-581. doi:10.1107/S090744490901169X

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Author Jacques, D. A.
Streamer, M
Rowland, S. L.
King, G. F.
Guss, J. M.
Trewhella, J
Langley, D. B.
Title Structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis and insights into its solution state
Journal name Acta Crystallographica Section D: Biological Crystallography   Check publisher's open access policy
ISSN 0907-4449
Publication date 2009-06-01
Year available 2009
Sub-type Article (original research)
DOI 10.1107/S090744490901169X
Open Access Status File (Publisher version)
Volume 65
Issue Part 6
Start page 574
End page 581
Total pages 8
Place of publication Malden, MA, United States
Publisher Wiley-Blackwell
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
060112 Structural Biology (incl. Macromolecular Modelling)
Abstract 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.
Keyword SMALL-ANGLE SCATTERING
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID FF0457488
511206
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
 
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Created: Thu, 03 Sep 2009, 18:07:53 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience