The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins.
YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-A resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.
Santelli
Eugenio
E
Division of Cellular Biology, Mail code MEM-116, Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Liddington
Robert C
RC
Mohan
Michael A
MA
Hoch
James A
JA
Szurmant
Hendrik
H
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D003460:Crystallization; D019281:Dimerization; D000071677:Histidine Kinase; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D011494:Protein Kinases / Q000378:metabolism; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D015398:Signal Transduction; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D011494:Protein Kinases; D000071677:Histidine Kinase