This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4lnn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4lnn| PDB=4lnn | SCENE= }}
 +
===B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS===
 +
{{ABSTRACT_PUBMED_24158439}}
-
The entry 4lnn is ON HOLD until Paper Publication
+
==About this Structure==
 +
[[4lnn]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNN OCA].
-
Authors: Schumacher, M.A., Chinnam, N., Tonthat, N., Fisher, S., Wray, L.
+
==Reference==
-
 
+
<ref group="xtra">PMID:024158439</ref><references group="xtra"/><references/>
-
Description: B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS
+
[[Category: Glutamate--ammonia ligase]]
 +
[[Category: Chinnam, N.]]
 +
[[Category: Fisher, S.]]
 +
[[Category: Schumacher, M A.]]
 +
[[Category: Tonthat, N.]]
 +
[[Category: Wray, L.]]
 +
[[Category: Alpha/beta]]
 +
[[Category: Dodecamer]]
 +
[[Category: Enzyme]]
 +
[[Category: Glutamine synthetase]]
 +
[[Category: Ligase]]

Revision as of 08:21, 13 November 2013

Template:STRUCTURE 4lnn

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of apo form of GS

Template:ABSTRACT PUBMED 24158439

About this Structure

4lnn is a 12 chain structure. Full crystallographic information is available from OCA.

Reference

  • Murray DS, Chinnam N, Tonthat NK, Whitfill T, Wray LV, Fisher SH, Schumacher MA. Structures of the B. subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism. J Biol Chem. 2013 Oct 24. PMID:24158439 doi:http://dx.doi.org/10.1074/jbc.M113.519496

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lnn"
Personal tools