Santelli Eugenio, Liddington Robert C, Mohan Michael A, Hoch James A, Szurmant Hendrik
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.
J Bacteriol. 2007 Apr;189(8):3290-5. doi: 10.1128/JB.01937-06. Epub 2007 Feb 16.
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.
YycI和YycH是两种膜锚定的周质蛋白,它们通过直接相互作用调节枯草芽孢杆菌必需的YycG组氨酸激酶。在此,我们展示了分辨率为2.9埃的YycI晶体结构。YycI形成二聚体,并且值得注意的是,尽管这两种蛋白质之间的序列同源性几乎检测不到(10%),但其结构类似于YycH的两个C端结构域的结构。