2GW8

Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 resolution

Summary for 2GW8

• Entry DOI: 10.2210/pdb2gw8/pdb
• Descriptor: PII signal transduction protein (2 entities in total)
• Functional Keywords: pii, signal transduction, transcriptional regulation, neisseria, structural genomics, oxford protein production facility, oppf, signaling protein
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 1
• Total formula weight: 12484.48

Authors

Nichols, C.E.,Sainsbury, S.,Berrow, N.S.,Alderton, D.,Stammers, D.K.,Owens, R.J.,Oxford Protein Production Facility (OPPF) (deposition date: 2006-05-04, release date: 2006-06-13, Last modification date: 2023-08-30)

Primary citation

Nichols, C.E.,Sainsbury, S.,Berrow, N.S.,Alderton, D.,Saunders, N.J.,Stammers, D.K.,Owens, R.J.
Structure of the P(II) signal transduction protein of Neisseria meningitidis at 1.85 A resolution.
Acta Crystallogr.,Sect.F, 62:494-497, 2006

PubMed Abstract: 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.

PubMed: 16754965
DOI: 10.1107/S1744309106015430

Experimental method

X-RAY DIFFRACTION (1.85 Å)