Structural highlights
Function
[YYCH_BACSU] Together with YycI, 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
The Bacillus subtilis YycFG two-component signal transduction system is essential for cell viability, and the YycH protein is part of the regulatory circuit that controls its activity. The crystal structure of YycH was solved by two-wavelength selenium anomalous dispersion data, and was refined using 2.3 A data to an R-factor of 25.2%. The molecule is made up of three domains, and has a novel three-dimensional structure. The N-terminal domain features a calcium binding site and the central domain contains two conserved loop regions.
The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure.,Szurmant H, Zhao H, Mohan MA, Hoch JA, Varughese KI Protein Sci. 2006 Apr;15(4):929-34. PMID:16600972[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
- ↑ Szurmant H, Zhao H, Mohan MA, Hoch JA, Varughese KI. The crystal structure of YycH involved in the regulation of the essential YycFG two-component system in Bacillus subtilis reveals a novel tertiary structure. Protein Sci. 2006 Apr;15(4):929-34. PMID:16600972 doi:15/4/929
