2c2a
From Proteopedia
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| , resolution 1.9Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN
Overview
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.
About this Structure
2C2A is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein., Marina A, Waldburger CD, Hendrickson WA, EMBO J. 2005 Dec 21;24(24):4247-59. Epub 2005 Dec 1. PMID:16319927
Page seeded by OCA on Sun Mar 23 14:49:50 2008
