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Structure of the N-Terminal Domain of Escherichia coli Glutamine Synthetase Adenylyltransferase

Xu, Yibin; Zhang, Rongguand; Joachimiak, Andrzej; Carr, Paul D; Vasudevan, Subhash; Ollis, David; Huber, Thomas


We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from...[Show more]

CollectionsANU Research Publications
Date published: 2004
Type: Journal article
Source: Structure
DOI: 10.1016/j.str.2004.02.029


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