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From Proteopedia
Crystal Structure of the sensor histidine kinase regulator YycI from Bacillus subtitlis
Structural highlights
FunctionYYCI_BACSU Together with YycH, regulates the activity of the two-component system YycF/YycG.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYycI 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. The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins.,Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H J Bacteriol. 2007 Apr;189(8):3290-5. Epub 2007 Feb 16. PMID:17307848[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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