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Title: Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 Ȃ resolution
Authors: Nichols, CE
Sainsbury, S
Berrow, NS
Alderton, D
Saunders, NJ
Stammers, DK
Owens, RJ
Keywords: PII signal transduction proteins;Neisseria meningitidis
Issue Date: 2006
Publisher: International Union of Crystallography
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(Pt 6): 494 - 497, Jun 2006
Abstract: The PII signal transduction proteins GlnB and GlnK are implicated in the regulation of nitrogen assimilation in Escherichia coli and other enteric bacteria. PII-like proteins are widely distributed in bacteria, archaea and plants. In contrast to other bacteria, Neisseria are limited to a single PII 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 PII protein from N. meningitidis (serotype B) has been solved by molecular replacement to a resolution of 1.85 Ȃ. Comparison of the structure with those of other PII 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 PII protein shares functions with GlnB/GlnK of enteric bacteria.
Description: Copyright @ 2006 International Union of Crystallography
ISSN: 1744-3091
Appears in Collections:Biological Sciences
Dept of Life Sciences Research Papers

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