1lm1: Difference between revisions

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{{STRUCTURE_1lm1|  PDB=1lm1  |  SCENE=  }}  
{{STRUCTURE_1lm1|  PDB=1lm1  |  SCENE=  }}  


'''Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme'''
===Structural studies on the synchronization of catalytic centers in glutamate synthase: native enzyme===




==Overview==
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The complex iron-sulfur flavoprotein glutamate synthase (GltS) plays a prominent role in ammonia assimilation in bacteria, yeasts, and plants. GltS catalyzes the formation of two molecules of l-glutamate from 2-oxoglutarate and l-glutamine via intramolecular channeling of ammonia. GltS has the impressive ability of synchronizing its distinct catalytic centers to avoid wasteful consumption of l-glutamine. We have determined the crystal structure of the ferredoxin-dependent GltS in several ligation and redox states. The structures reveal the crucial elements in the synchronization between the glutaminase site and the 2-iminoglutarate reduction site. The structural data combined with the catalytic properties of GltS indicate that binding of ferredoxin and 2-oxoglutarate to the FMN-binding domain of GltS induce a conformational change in the loop connecting the two catalytic centers. The rearrangement induces a shift in the catalytic elements of the amidotransferase domain, such that it becomes activated. This machinery, over a distance of more than 30 A, controls the ability of the enzyme to bind and hydrolyze the ammonia-donating substrate l-glutamine.
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{{ABSTRACT_PUBMED_11967268}}


==About this Structure==
==About this Structure==
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[[Category: Channeling]]
[[Category: Channeling]]
[[Category: Glutamate synthase]]
[[Category: Glutamate synthase]]
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