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PMID:9989504
| Citation |
Bilwes, AM, Alex, LA, Crane, BR and Simon, MI (1999) Structure of CheA, a signal-transducing histidine kinase. Cell 96:131-41 |
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| 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. |
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| Keywords |
Adenosine Triphosphatases/chemistry; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Dimerization; Hydrolysis; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Protein Conformation; Protein Kinases/chemistry; Protein Kinases/metabolism; Sequence Homology, Amino Acid; Signal Transduction; Thermotoga maritima/enzymology |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0016301: kinase activity |
ECO:0000255: |
UniProtKB:Q56310
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F |
Figure 1 shows a schematic design of CheA histidine kinase based upon the position of the sequence of the substrate histidine (H box) with respect to the kinase domain. CheW is shown in this design, but it is actually a coupling protein that interacts with the sensor and CheA. |
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See also
References
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