2C2A

Structure of the entire cytoplasmic portion of a sensor histidine kinase protein

Summary for 2C2A

• Entry DOI: 10.2210/pdb2c2a/pdb
• Descriptor: SENSOR HISTIDINE KINASE, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: histidine kinase, phosphotransfer, phoq, selenomethionyl mad, two-component systems, transferase
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 1
• Total formula weight: 29933.61

Authors

Marina, A.,Waldburger, C.D.,Hendrickson, W.A. (deposition date: 2005-09-27, release date: 2005-11-21, Last modification date: 2024-10-23)

Primary citation

Marina, A.,Waldburger, C.D.,Hendrickson, W.A.
Structure of the Entire Cytoplasmic Portion of a Sensor Histidine-Kinase Protein.
Embo J., 24:4247-, 2005

PubMed Abstract: The large majority of histidine kinases (HKs) are multifunctional enzymes having autokinase, phosphotransfer and phosphatase activities, and most of these are transmembrane sensor proteins. Sensor HKs possess conserved cytoplasmic phosphorylation and ATP-binding kinase domains. The different enzymatic activities require participation by one or both of these domains, implying the need for different conformational states. The catalytic domains are linked to the membrane through a coiled-coil segment that sometimes includes other domains. We describe here the first crystal structure of the complete cytoplasmic region of a sensor HK, one from the thermophile Thermotoga maritima in complex with ADPbetaN at 1.9 A resolution. The structure reveals previously unidentified functions for several conserved residues and reveals the relative disposition of domains in a state seemingly poised for phosphotransfer. The structure thereby inspires hypotheses for the mechanisms of autophosphorylation, phosphotransfer and response-regulator dephosphorylation, and for signal transduction through the coiled-coil segment. Mutational tests support the functional relevance of interdomain contacts.

PubMed: 16319927
DOI: 10.1038/SJ.EMBOJ.7600886

Experimental method

X-RAY DIFFRACTION (1.9 Å)