2ZP2

C-terminal domain of KipI from Bacillus subtilis

Summary for 2ZP2

• Entry DOI: 10.2210/pdb2zp2/pdb
• Descriptor: Kinase A inhibitor (1 entity in total)
• Functional Keywords: kipi, histidine kinase inhibitor, atp-binding, nucleotide-binding, protein kinase inhibitor, sporulation, transferase inhibitor
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 30683.06

Authors

Langley, D.B.,Jacques, D.A. (deposition date: 2008-06-24, release date: 2009-01-20, Last modification date: 2023-11-01)

Primary citation

Jacques, D.A.,Langley, D.B.,Jeffries, C.M.,Cunningham, K.A.,Burkholder, W.F.,Guss, J.M.,Trewhella, J.
Histidine kinase regulation by a cyclophilin-like inhibitor
J.Mol.Biol., 384:422-435, 2008

PubMed Abstract: The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a conserved proline in the KinA dimerization and histidine-phosphotransfer (DHp) domain. Our crystal structure of the KipI C-domain reveals the binding motif has a distinctive hydrophobic groove formed by a five-stranded antiparallel beta-sheet; a characteristic of the cyclophilin family of proteins that bind prolines and often act as cis-trans peptidyl-prolyl isomerases. We propose that the DHp domain of KinA transmits conformational signals to regulate kinase activity via this proline-mediated interaction. Given that both KinA and KipI homologues are widespread in the bacterial kingdom, this mechanism has broad significance in bacterial signal transduction.

PubMed: 18823995
DOI: 10.1016/j.jmb.2008.09.017

Experimental method

X-RAY DIFFRACTION (3.01 Å)