Extracytoplasmic PAS-like domains are common in signal transduction proteins.
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.
Chang
Changsoo
C
Biosciences Division, Argonne National Laboratory, Argonne, Illinois 60439, USA.
Tesar
Christine
C
Gu
Minyi
M
Babnigg
Gyorgy
G
Joachimiak
Andrzej
A
Pokkuluri
P Raj
PR
Szurmant
Hendrik
H
Schiffer
Marianne
M
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000737:chemistry* / Q000235:genetics; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D001426:Bacterial Proteins; C061279:PhoR protein, Bacteria; D011494:Protein Kinases