Structural Basis for Morpheein-type Allosteric Regulation of Escherichia coli Glucosamine-6-phosphate Synthase: EQUILIBRIUM BETWEEN INACTIVE HEXAMER AND ACTIVE DIMER

The amino-terminal cysteine of glucosamine-6-phosphate synthase (GlmS) acts as a nucleophile to release and transfer ammonia from glutamine to fructose 6-phosphate through a channel. The crystal structure of the C1A mutant of Escherichia coli GlmS, solved at 2.5 Å resolution, is organized as a hexam...

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Bibliografiske detaljer
Main Authors: Mouilleron, Stéphane, Badet-Denisot, Marie-Ange, Pecqueur, Ludovic, Madiona, Karine, Assrir, Nadine, Badet, Bernard, Golinelli-Pimpaneau, Béatrice
Format: Artigo
Sprog:Inglês
Udgivet: American Society for Biochemistry and Molecular Biology 2012
Fag:
Enzymology
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3464560/
https://ncbi.nlm.nih.gov/pubmed/22851174
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M112.380378
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