Structural highlights
Function
[YYCI_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 PubMed
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.
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
- ↑ Szurmant H, Mohan MA, Imus PM, Hoch JA. YycH and YycI interact to regulate the essential YycFG two-component system in Bacillus subtilis. J Bacteriol. 2007 Apr;189(8):3280-9. Epub 2007 Feb 16. PMID:17307850 doi:http://dx.doi.org/10.1128/JB.01936-06
- ↑ Szurmant H, Bu L, Brooks CL 3rd, Hoch JA. An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5891-6. doi:, 10.1073/pnas.0800247105. Epub 2008 Apr 11. PMID:18408157 doi:http://dx.doi.org/10.1073/pnas.0800247105
- ↑ Santelli E, Liddington RC, Mohan MA, Hoch JA, Szurmant H. The crystal structure of Bacillus subtilis YycI reveals a common fold for two members of an unusual class of sensor histidine kinase regulatory proteins. J Bacteriol. 2007 Apr;189(8):3290-5. Epub 2007 Feb 16. PMID:17307848 doi:10.1128/JB.01937-06
