1i5b
STRUCTURE OF CHEA DOMAIN P4 IN COMPLEX WITH ADPNP AND MANGANESE
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OverviewOverview
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.
About this StructureAbout this Structure
1I5B is a Single protein structure of sequence from Thermotoga maritima with ACT, MN and ANP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Nucleotide binding by the histidine kinase CheA., Bilwes AM, Quezada CM, Croal LR, Crane BR, Simon MI, Nat Struct Biol. 2001 Apr;8(4):353-60. PMID:11276258
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