3CWF

Crystal structure of PAS domain of two-component sensor histidine kinase

Summary for 3CWF

• Entry DOI: 10.2210/pdb3cwf/pdb
• Descriptor: Alkaline phosphatase synthesis sensor protein phoR, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: bacillus subtilis, pas domain, alkaline phosphatase synthesis sensor protein phor, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, kinase, membrane, phosphate transport, phosphoprotein, transferase, transmembrane, transport, two-component regulatory system
• Biological source: Bacillus subtilis subsp. subtilis
• Cellular location: Cell membrane; Multi-pass membrane protein (Probable): P23545
• Total number of polymer chains: 2
• Total formula weight: 26442.92

Authors

Chang, C.,Tesar, C.,Gu, M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2008-04-21, release date: 2008-05-06, Last modification date: 2024-02-21)

Primary citation

Chang, C.,Tesar, C.,Gu, M.,Babnigg, G.,Joachimiak, A.,Pokkuluri, P.R.,Szurmant, H.,Schiffer, M.
Extracytoplasmic PAS-like domains are common in signal transduction proteins.
J.Bacteriol., 192:1156-1159, 2010

PubMed Abstract: We present the crystal structure of the extracytoplasmic domain of the Bacillus subtilis PhoR sensor histidine kinase, part of a two-component system involved in adaptation to low environmental phosphate concentrations. In addition to the PhoR structure, we predict that the majority of the extracytoplasmic domains of B. subtilis sensor kinases will adopt a fold similar to the ubiquitous PAS domain.

PubMed: 20008068
DOI: 10.1128/JB.01508-09

Experimental method

X-RAY DIFFRACTION (2.2 Å)