1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis

Hynson, Robert M. G., Kwan, Ann H., Jacques, David A., Mackay, Joel P. and Trewhella, Jill (2010) 1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis. Biomolecular NMR Assignments, 4 2: 167-169. doi:10.1007/s12104-010-9237-6


Author Hynson, Robert M. G.
Kwan, Ann H.
Jacques, David A.
Mackay, Joel P.
Trewhella, Jill
Title 1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis
Formatted title
1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis
Journal name Biomolecular NMR Assignments   Check publisher's open access policy
ISSN 1874-2718
1874-270X
Publication date 2010-10
Sub-type Article (original research)
DOI 10.1007/s12104-010-9237-6
Volume 4
Issue 2
Start page 167
End page 169
Total pages 4
Place of publication Dordrecht, Netherlands
Publisher Springer
Language eng
Formatted abstract
KipI is a sporulation inhibitor in Bacillus subtilis which acts by binding to the dimerisation and histidine phosphotransfer (DHp) domain of KinA, the principle input kinase in the phosphorelay responsible for sporulation. The 15N, 13C and 1H chemical shift assignments of the N-terminal domain of KipI were determined using multidimensional, multinuclear NMR experiments. The N-terminal domain has two conformers and resonance assignments have been made for both conformers.
Keyword Bacterial signal transduction
KipI
Histidine kinase inhibition
Bacillus subtilis
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Institute for Molecular Bioscience - Publications
 
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Created: Wed, 25 Jul 2012, 10:47:56 EST by Susan Allen on behalf of Institute for Molecular Bioscience