2pl1

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spinqualitylabelsall models 2pl1, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Berrylium Fluoride activated receiver domain of E.coli PhoP

Overview

The response regulator PhoP is part of the PhoQ/PhoP two-component system, involved in responses to depletion of extracellular Mg(2+). Here, we, report the crystal structures of the receiver domain of Escherichia coli, PhoP determined in the absence and presence of the phosphoryl analog, beryllofluoride. In the presence of beryllofluoride, the active receiver, domain forms a twofold symmetric dimer similar to that seen in structures, of other regulatory domains from the OmpR/PhoB family, providing further, evidence that members of this family utilize a common mode of dimerization, in the active state. In the absence of activating agents, the PhoP, receiver domain crystallizes with a similar structure, consistent with the, previous observation that high concentrations can promote an active state, of PhoP independent of phosphorylation.

About this Structure

2PL1 is a Single protein structure of sequence from Escherichia coli with PT, MG and BEF as ligands. This structure superseeds the now removed PDB entry 2EUB. Full crystallographic information is available from OCA.

Reference

Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog Beryllofluoride., Bachhawat P, Stock AM, J Bacteriol. 2007 Aug;189(16):5987-95. Epub 2007 Jun 1. PMID:17545283

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