Structure of the N-Terminal domain of Escherichia coli glutamine synthetase adenylyltransferase

Xu, Yibin, Zhang, Rongguand, Joachimiak, Andrzej, Carr, Paul D., Huber, Thomas, Vasudevan, Subhash G., and Ollis, David L. (2004) Structure of the N-Terminal domain of Escherichia coli glutamine synthetase adenylyltransferase. Structure, 12 (5). pp. 861-869.

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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 that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase β, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polβ-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.

Item ID: 13945
Item Type: Article (Research - C1)
ISSN: 1878-4186
Keywords: nitrogen fixation
Date Deposited: 11 Nov 2010 01:42
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060199 Biochemistry and Cell Biology not elsewhere classified @ 100%
SEO Codes: 82 PLANT PRODUCTION AND PLANT PRIMARY PRODUCTS > 8205 Winter Grains and Oilseeds > 820503 Grain Legumes @ 100%
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