4I5S

Structure and function of sensor histidine kinase

Summary for 4I5S

• Entry DOI: 10.2210/pdb4i5s/pdb
• Descriptor: Putative histidine kinase CovS; VicK-like protein (1 entity in total)
• Functional Keywords: histidine kinase, vick, hamp, pas, transferase, kinase, phosphorylation
• Biological source: Streptococcus mutans serotype c
• Total number of polymer chains: 2
• Total formula weight: 103504.17

Authors

Cai, Y. (deposition date: 2012-11-28, release date: 2013-03-27, Last modification date: 2024-03-20)

Primary citation

Wang, C.,Sang, J.,Wang, J.,Su, M.,Downey, J.S.,Wu, Q.,Wang, S.,Cai, Y.,Xu, X.,Wu, J.,Senadheera, D.B.,Cvitkovitch, D.G.,Chen, L.,Goodman, S.D.,Han, A.
Mechanistic insights revealed by the crystal structure of a histidine kinase with signal transducer and sensor domains
Plos Biol., 11:e1001493-e1001493, 2013

PubMed Abstract: Two-component systems (TCSs) are important for the adaptation and survival of bacteria and fungi under stress conditions. A TCS is often composed of a membrane-bound sensor histidine kinase (SK) and a response regulator (RR), which are relayed through sequential phosphorylation steps. However, the mechanism for how an SK is switched on in response to environmental stimuli remains obscure. Here, we report the crystal structure of a complete cytoplasmic portion of an SK, VicK from Streptococcus mutans. The overall structure of VicK is a long-rod dimer that anchors four connected domains: HAMP, Per-ARNT-SIM (PAS), DHp, and catalytic and ATP binding domain (CA). The HAMP, a signal transducer, and the PAS domain, major sensor, adopt canonical folds with dyad symmetry. In contrast, the dimer of the DHp and CA domains is asymmetric because of different helical bends in the DHp domain and spatial positions of the CA domains. Moreover, a conserved proline, which is adjacent to the phosphoryl acceptor histidine, contributes to helical bending, which is essential for the autokinase and phosphatase activities. Together, the elegant architecture of VicK with a signal transducer and sensor domain suggests a model where DHp helical bending and a CA swing movement are likely coordinated for autokinase activation.

PubMed: 23468592
DOI: 10.1371/journal.pbio.1001493

Experimental method

X-RAY DIFFRACTION (3.3 Å)