2gw8
From Proteopedia
(New page: 200px<br /><applet load="2gw8" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gw8, resolution 1.85Å" /> '''Structure of the PII...) |
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==Overview== | ==Overview== | ||
| - | The P(II) signal transduction proteins GlnB and GlnK are implicated in the | + | 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. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 A resolution., Nichols CE, Sainsbury S, Berrow NS, Alderton D, Saunders NJ, Stammers DK, Owens RJ, Acta | + | Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 A resolution., Nichols CE, Sainsbury S, Berrow NS, Alderton D, Saunders NJ, Stammers DK, Owens RJ, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):494-7. Epub 2006 May 31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16754965 16754965] |
[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Alderton, D.]] | [[Category: Alderton, D.]] | ||
| - | [[Category: Berrow, N | + | [[Category: Berrow, N S.]] |
| - | [[Category: Nichols, C | + | [[Category: Nichols, C E.]] |
| - | [[Category: OPPF, Oxford | + | [[Category: OPPF, Oxford Protein Production Facility.]] |
| - | [[Category: Owens, R | + | [[Category: Owens, R J.]] |
[[Category: Sainsbury, S.]] | [[Category: Sainsbury, S.]] | ||
| - | [[Category: Stammers, D | + | [[Category: Stammers, D K.]] |
[[Category: neisseria]] | [[Category: neisseria]] | ||
[[Category: oppf]] | [[Category: oppf]] | ||
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[[Category: transcriptional regulation]] | [[Category: transcriptional regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:36:03 2008'' |
Revision as of 15:36, 21 February 2008
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Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 resolution
Overview
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.
About this Structure
2GW8 is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.
Reference
Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 A resolution., Nichols CE, Sainsbury S, Berrow NS, Alderton D, Saunders NJ, Stammers DK, Owens RJ, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):494-7. Epub 2006 May 31. PMID:16754965
Page seeded by OCA on Thu Feb 21 17:36:03 2008
Categories: Neisseria meningitidis | Single protein | Alderton, D. | Berrow, N S. | Nichols, C E. | OPPF, Oxford Protein Production Facility. | Owens, R J. | Sainsbury, S. | Stammers, D K. | Neisseria | Oppf | Oxford protein production facility | Pii | Signal transduction | Structural genomics | Transcriptional regulation
