1I58

STRUCTURE OF THE HISTIDINE KINASE CHEA ATP-BINDING DOMAIN IN COMPLEX WITH ATP ANALOG ADPCP AND MAGNESIUM

Summary for 1I58

• Entry DOI: 10.2210/pdb1i58/pdb
• Related: 1B3Q
• Descriptor: CHEMOTAXIS PROTEIN CHEA, ACETATE ION, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: beta-alpha sandwich, signaling protein, transferase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 43233.34

Authors

Bilwes, A.M.,Quezada, C.M.,Croal, L.R.,Crane, B.R.,Simon, M.I. (deposition date: 2001-02-26, release date: 2001-08-26, Last modification date: 2023-08-09)

Primary citation

Bilwes, A.M.,Quezada, C.M.,Croal, L.R.,Crane, B.R.,Simon, M.I.
Nucleotide binding by the histidine kinase CheA.
Nat.Struct.Biol., 8:353-360, 2001

PubMed Abstract: To probe the structural basis for protein histidine kinase (PHK) catalytic activity and the prospects for PHK-specific inhibitor design, we report the crystal structures for the nucleotide binding domain of Thermotoga maritima CheA with ADP and three ATP analogs (ADPNP, ADPCP and TNP-ATP) bound with either Mg(2+) or Mn(2+). The conformation of ADPNP bound to CheA and related ATPases differs from that reported in the ADPNP complex of PHK EnvZ. Interactions of the active site with the nucleotide gamma-phosphate and its associated Mg(2+) ion are linked to conformational changes in an ATP-lid that could mediate recognition of the substrate domain. The inhibitor TNP-ATP binds CheA with its phosphates in a nonproductive conformation and its adenine and trinitrophenyl groups in two adjacent binding pockets. The trinitrophenyl interaction may be exploited for designing CheA-targeted drugs that would not interfere with host ATPases.

PubMed: 11276258
DOI: 10.1038/86243

Experimental method

X-RAY DIFFRACTION (1.6 Å)