2gw8: Difference between revisions

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[[Image:2gw8.~~gif~~|left|200px]]

[[Image:2gw8.png|left|200px]]

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

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

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16754965}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16754965 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural genomic]]

[[Category: Transcriptional regulation]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 05~~:36:53 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:02:45 2008''

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-[[Image:2gw8.gif|left|200px]]
+{{Seed}}
+[[Image:2gw8.png|left|200px]]
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 {{STRUCTURE_2gw8|  PDB=2gw8  |  SCENE=  }}
-'''Structure of the PII signal transduction protein of Neisseria meningitidis at 1.85 resolution'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16754965}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16754965 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16754965}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Transcriptional regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:36:53 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:02:45 2008''