4c3m
From Proteopedia
(Difference between revisions)
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- | + | {{STRUCTURE_4c3m| PDB=4c3m | SCENE= }} | |
+ | ===Structure of wildtype PII from S. elongatus at medium 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== | |
- | + | [[4c3m]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3M OCA]. | |
- | + | [[Category: Forchhammer, K.]] | |
+ | [[Category: Zeth, K.]] | ||
+ | [[Category: Transcription]] |
Revision as of 05:14, 13 February 2014
Structure of wildtype PII from S. elongatus at medium resolution
Function
[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
4c3m is a 3 chain structure. Full crystallographic information is available from OCA.