1B3Q

CRYSTAL STRUCTURE OF CHEA-289, A SIGNAL TRANSDUCING HISTIDINE KINASE

Summary for 1B3Q

• Entry DOI: 10.2210/pdb1b3q/pdb
• Descriptor: PROTEIN (CHEMOTAXIS PROTEIN CHEA), MERCURY (II) ION (3 entities in total)
• Functional Keywords: histine kinase, signal transduction, chemotaxis, multi-domains protein, transferase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 85329.86

Authors

Bilwes, A.M.,Alex, L.A.,Crane, B.R.,Simon, M.I. (deposition date: 1998-12-14, release date: 1999-12-15, Last modification date: 2023-12-27)

Primary citation

Bilwes, A.M.,Alex, L.A.,Crane, B.R.,Simon, M.I.
Structure of CheA, a signal-transducing histidine kinase.
Cell(Cambridge,Mass.), 96:131-141, 1999

PubMed Abstract: Histidine kinases allow bacteria, plants, and fungi to sense and respond to their environment. The 2.6 A resolution crystal structure of Thermotoga maritima CheA (290-671) histidine kinase reveals a dimer where the functions of dimerization, ATP binding, and regulation are segregated into domains. The kinase domain is unlike Ser/Thr/Tyr kinases but resembles two ATPases, Gyrase B and Hsp90. Structural analogies within this superfamily suggest that the P1 domain of CheA provides the nucleophilic histidine and activating glutamate for phosphotransfer. The regulatory domain, which binds the homologous receptor-coupling protein CheW, topologically resembles two SH3 domains and provides different protein recognition surfaces at each end. The dimerization domain forms a central four-helix bundle about which the kinase and regulatory domains pivot on conserved hinges to modulate transphosphorylation. Different subunit conformations suggest that relative domain motions link receptor response to kinase activity.

PubMed: 9989504
DOI: 10.1016/S0092-8674(00)80966-6

Experimental method

X-RAY DIFFRACTION (2.6 Å)