4c3l: Difference between revisions
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{{STRUCTURE_4c3l| PDB=4c3l | SCENE= }} | |||
===Structure of wildtype PII from S. elongatus at high resolution=== | |||
==Function== | |||
[[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. | |||
==About this Structure== | |||
[[4c3l]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3L OCA]. | |||
[[Category: Forchhammer, K.]] | |||
[[Category: Zeth, K.]] | |||
[[Category: Transcription]] |
Revision as of 11:21, 15 January 2014
Structure of wildtype PII from S. elongatus at high resolutionStructure of wildtype PII from S. elongatus at high resolution
FunctionFunction
[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.
About this StructureAbout this Structure
4c3l is a 1 chain structure. Full crystallographic information is available from OCA.