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DC Field | Value | Language |
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dc.contributor.author | Nichols, CE | - |
dc.contributor.author | Sainsbury, S | - |
dc.contributor.author | Berrow, NS | - |
dc.contributor.author | Alderton, D | - |
dc.contributor.author | Saunders, NJ | - |
dc.contributor.author | Stammers, DK | - |
dc.contributor.author | Owens, RJ | - |
dc.date.accessioned | 2012-09-14T12:36:20Z | - |
dc.date.available | 2012-09-14T12:36:20Z | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(Pt 6): 494 - 497, Jun 2006 | en_US |
dc.identifier.issn | 1744-3091 | - |
dc.identifier.uri | http://onlinelibrary.wiley.com/doi/10.1107/S1744309106015430/abstract | en |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/6648 | - |
dc.description | Copyright @ 2006 International Union of Crystallography | en_US |
dc.description.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. | en_US |
dc.description.sponsorship | This study is funded by the Medical Research Council UK and Europe (SPINE) consortium (European Commission Grant No. QLG2-CT-2002-00988). | en_US |
dc.language.iso | en | en_US |
dc.publisher | International Union of Crystallography | en_US |
dc.subject | PII signal transduction proteins | en_US |
dc.subject | Neisseria meningitidis | en_US |
dc.title | Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 Ȃ resolution | en_US |
dc.type | Article | en_US |
dc.identifier.doi | http://dx.doi.org/10.1107/S1744309106015430 | - |
pubs.organisational-data | /Brunel | - |
pubs.organisational-data | /Brunel/Brunel Active Staff | - |
pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care | - |
pubs.organisational-data | /Brunel/Brunel Active Staff/School of Health Sciences & Social Care/Biological Sciences | - |
pubs.organisational-data | /Brunel/Group Publication Pages | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups | - |
pubs.organisational-data | /Brunel/University Research Centres and Groups/School of Health Sciences and Social Care - URCs and Groups/Centre for Systems and Synthetic Biology | - |
Appears in Collections: | Biological Sciences Publications Dept of Life Sciences Research Papers |
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