Journal article

Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.

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

Structure | Published : 2004

Abstract

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 beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding resi..

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University of Melbourne Researchers