Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 Å resolution
Creators
- 1. Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN (United Kingdom)
- 2. The Oxford Protein Production Facility, Henry Wellcome Building for Genomic Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN (United Kingdom)
- 3. The Bacterial Pathogenesis and Functional Genomics Group, The Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE (United Kingdom)
Description
The structure of the PII signal transduction protein of N. meningitidis at 1.85 Å resolution is described. 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 Å. 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
Availability note (English)
Available from http://dx.doi.org/10.1107/S1744309106015430; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2243107Additional details
Identifiers
- URL
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2243107;
- DOI
- 10.1107/S1744309106015430;
- PII
- S1744309106015430;
Publishing Information
- Journal Title
- Acta Crystallographica. Section F
- Journal Volume
- 62
- Journal Issue
- Pt 6
- Journal Page Range
- p. 494-497
- ISSN
- 1744-3091
- CODEN
- ACSFCL
INIS
- Country of Publication
- United Kingdom
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 46065519
- Subject category
- S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
- Descriptors DEI
- ESCHERICHIA COLI; NITROGEN; PROTEINS; RESOLUTION; SIGNALS
- Descriptors DEC
- BACTERIA; ELEMENTS; MICROORGANISMS; NONMETALS; ORGANIC COMPOUNDS
Optional Information
- Copyright
- Copyright (c) International Union of Crystallography 2006
- Notes
- PMCID: PMC2243107; PMID: 16754965; PUBLISHER-ID: sw5006; OAI: oai:pubmedcentral.nih.gov:2243107; This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.