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4c3l

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3l RCSB], [http://www.ebi.ac.uk/pdbsum/4c3l PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3l RCSB], [http://www.ebi.ac.uk/pdbsum/4c3l PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GLNB_SYNE7 GLNB_SYNE7]] P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is phosphorylated, these events are reversed. In nitrogen-limiting conditions, when the ratio of Gln to 2-ketoglutarate decreases, P-II is phosphorylated which allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 09:24, 25 December 2014

Structure of wildtype PII from S. elongatus at high resolution

4c3l, resolution 1.60Å

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