3D36
How to Switch Off a Histidine Kinase: Crystal Structure of Geobacillus stearothermophilus KinB with the Inhibitor Sda
Summary for 3D36
| Entry DOI | 10.2210/pdb3d36/pdb |
| Descriptor | Sporulation kinase B, Sporulation kinase inhibitor Sda, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | ghkl atpase, four helix bundle, class i two-component histidine kinase, kinase, phosphoprotein, transferase, two-component regulatory system, transferase-transferase inhibitor complex, transferase/transferase inhibitor |
| Biological source | Geobacillus stearothermophilus More |
| Total number of polymer chains | 3 |
| Total formula weight | 60894.81 |
| Authors | Bick, M.J.,Lamour, V.,Rajashankar, K.R.,Gordiyenko, Y.,Robinson, C.V.,Darst, S.A. (deposition date: 2008-05-09, release date: 2009-01-13, Last modification date: 2024-02-21) |
| Primary citation | Bick, M.J.,Lamour, V.,Rajashankar, K.R.,Gordiyenko, Y.,Robinson, C.V.,Darst, S.A. How to switch off a histidine kinase: crystal structure of Geobacillus stearothermophilus KinB with the inhibitor Sda J.Mol.Biol., 386:163-177, 2009 Cited by PubMed Abstract: 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. PubMed: 19101565DOI: 10.1016/j.jmb.2008.12.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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