4c3m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4c3m| PDB=4c3m | SCENE= }}
 +
===Structure of wildtype PII from S. elongatus at medium resolution===
-
The entry 4c3m is ON HOLD
+
==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.
-
Authors: Zeth, K., Forchhammer, K.
+
==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].
-
Description: Structure of wildtype PII from S. elongatus at medium resolution
+
[[Category: Forchhammer, K.]]
 +
[[Category: Zeth, K.]]
 +
[[Category: Transcription]]

Revision as of 05:14, 13 February 2014

Template:STRUCTURE 4c3m

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.

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools