4lno: Difference between revisions
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{{STRUCTURE_4lno| PDB=4lno | SCENE= }} | |||
===B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1=== | |||
{{ABSTRACT_PUBMED_24158439}} | |||
==About this Structure== | |||
[[4lno]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LNO OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024158439</ref><references group="xtra"/><references/> | |||
[[Category: Glutamate--ammonia ligase]] | |||
[[Category: Chinnam, N.]] | |||
[[Category: Fisher, S.]] | |||
[[Category: Schumacher, M A.]] | |||
[[Category: Tonthat, N.]] | |||
[[Category: Wray, L.]] | |||
[[Category: Alpha/beta]] | |||
[[Category: Glnr]] | |||
[[Category: Ligase]] | |||
[[Category: Tnra]] | |||
Revision as of 08:17, 13 November 2013
B. subtilis glutamine synthetase structures reveal large active site conformational changes and basis for isoenzyme specific regulation: form two of GS-1
Template:ABSTRACT PUBMED 24158439
About this Structure
4lno is a 6 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:https://dx.doi.org/10.1074/jbc.M113.519496