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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.

Original publication

DOI

10.1107/S1744309106015430

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/06/2006

Volume

62

Pages

494 - 497

Keywords

Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Escherichia coli Proteins, Molecular Structure, Neisseria meningitidis, Nucleotidyltransferases, PII Nitrogen Regulatory Proteins, Protein Conformation, Sequence Homology, Amino Acid, Signal Transduction