4lnk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
{{STRUCTURE_4lnk| PDB=4lnk | SCENE= }}
{{STRUCTURE_4lnk| PDB=4lnk | SCENE= }}
===B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex===
===B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex===
 +
{{ABSTRACT_PUBMED_24158439}}
==About this Structure==
==About this Structure==
-
[[4lnk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNK OCA].
+
[[4lnk]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNK OCA].
-
[[Category: Bacillus subtilis]]
+
 
 +
==Reference==
 +
<ref group="xtra">PMID:024158439</ref><references group="xtra"/><references/>
 +
[[Category: Bacillus globigii migula 1900]]
[[Category: Glutamate--ammonia ligase]]
[[Category: Glutamate--ammonia ligase]]
[[Category: Chinnam, N.]]
[[Category: Chinnam, N.]]

Revision as of 06:29, 13 November 2013

Template:STRUCTURE 4lnk

B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: structure of GS-glutamate-AMPPCP complex

Template:ABSTRACT PUBMED 24158439

About this Structure

4lnk is a 6 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. 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

Personal tools