4lnk: Difference between revisions
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{{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/ | [[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 | |||
==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
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:https://dx.doi.org/10.1074/jbc.M113.519496
