Nichols Charles E, Sainsbury Sarah, Berrow Nick S, Alderton David, Saunders Nigel J, Stammers David K, Owens Raymond J
Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):494-7. doi: 10.1107/S1744309106015430. Epub 2006 May 31.
The P(II) signal transduction proteins GlnB and GlnK are implicated in the regulation of nitrogen assimilation in Escherichia coli and other enteric bacteria. P(II)-like proteins are widely distributed in bacteria, archaea and plants. In contrast to other bacteria, Neisseria are limited to a single P(II) protein (NMB 1995), which shows a high level of sequence identity to GlnB and GlnK from Escherichia coli (73 and 62%, respectively). The structure of the P(II) protein from N. meningitidis (serotype B) has been solved by molecular replacement to a resolution of 1.85 A. Comparison of the structure with those of other P(II) proteins shows that the overall fold is tightly conserved across the whole population of related proteins, in particular the positions of the residues implicated in ATP binding. It is proposed that the Neisseria P(II) protein shares functions with GlnB/GlnK of enteric bacteria.
P(II)信号转导蛋白GlnB和GlnK参与大肠杆菌及其他肠道细菌中氮同化的调控。类P(II)蛋白广泛分布于细菌、古菌和植物中。与其他细菌不同,奈瑟菌仅有一种P(II)蛋白(NMB 1995),该蛋白与大肠杆菌的GlnB和GlnK具有高度的序列同一性(分别为73%和62%)。通过分子置换法解析了脑膜炎奈瑟菌(B血清型)P(II)蛋白的结构,分辨率达到1.85 Å。将该结构与其他P(II)蛋白的结构进行比较,结果表明在整个相关蛋白群体中,整体折叠结构高度保守,特别是与ATP结合相关的残基位置。有人提出奈瑟菌P(II)蛋白与肠道细菌的GlnB/GlnK具有共同功能。