4cti

Escherichia coli EnvZ histidine kinase catalytic part fused to Archaeoglobus fulgidus Af1503 HAMP domain

spinqualitylabelsall models 4cti, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cti is a 4 chain structure with sequence from Archaeoglobus fulgidus and Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.847Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function O28769_ARCFU ENVZ_ECOLI Member of the two-component regulatory system EnvZ/OmpR involved in the regulation of osmoregulation (genes ompF and ompC). EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals. Publication Abstract from PubMed Sensor histidine kinases are important sensors of the extracellular environment and relay signals via conformational changes that trigger autophosphorylation of the kinase and subsequent phosphorylation of a response regulator. The exact mechanism and the regulation of this protein family are a matter of ongoing investigation. Here we present a crystal structure of a functional chimeric protein encompassing the entire catalytic part of the Escherichia coli EnvZ histidine kinase, fused to the HAMP domain of the Archaeoglobus fulgidus Af1503 receptor. The construct is thus equivalent to the full cytosolic part of EnvZ. The structure shows a putatively active conformation of the catalytic domain and gives insight into how this conformation could be brought about in response to sensory input. Our analysis suggests a sequential flip-flop autokinase mechanism. Crystallographic snapshot of the Escherichia coli EnvZ histidine kinase in an active conformation.,Ferris HU, Coles M, Lupas AN, Hartmann MD J Struct Biol. 2014 Mar 26. pii: S1047-8477(14)00067-7. doi:, 10.1016/j.jsb.2014.03.014. PMID:24681325 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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