ANSTO Publications Online >
Journal Publications >
Journal Articles >

Please use this identifier to cite or link to this item: http://apo.ansto.gov.au/dspace/handle/10238/1108

Title: Structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition.
Authors: Whitten, AE
Jacques, DA
Hammouda, B
Hanley, TL
King, GF
Guss, JM
Trewhella, J
Langley, DB
Keywords: Phosphotransferases
Histidine
Inhibition
Proteins
Small Angle Scattering
DNA
Issue Date: 27-Apr-2007
Publisher: Elsevier
Citation: Whitten, A. E., Jacques, D. A., Hammouda, B., Hanley, T., King, G. F., Guss, J. M., et al. (2007). The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. Journal of Molecular Biology, 368(2), 407-420.
Abstract: The Bacillus subtilis histidine kinase KinA controls activation of the transcription factor governing sporulation, SpoOA. The decision to sporulate involves KinA phosphorylating itself on a conserved histidine residue, after which the phosphate moiety is relayed via two other proteins to SpoOA. The DNA-damage checkpoint inhibitor Sda halts this pathway by binding KinA and blocking the autokinase reaction. We have performed small-angle X-ray scattering and neutron contrast variation studies on the complex formed by KinA and Sda. The data show that two Sda molecules bind to the base of the DHp dimerization domain of the KinA dimer. In this position Sda does riot appear to be able to sterically block the catalytic domain from accessing its target histidine, as previously proposed, but rather may effect an allosteric mode of inhibition involving transmission of the inhibitory signal via the four-helix bundle that forms the DHp domain. © 2007, Elsevier Ltd.
URI: http://dx.doi.org/10.1016/j.jmb.2007.01.064
http://apo.ansto.gov.au/dspace/handle/10238/1108
ISSN: 0022-2836
Appears in Collections:Journal Articles

Files in This Item:

There are no files associated with this item.

Items in APO are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback