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

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    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 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.

    Original languageEnglish
    Pages (from-to)861-869
    Number of pages9
    JournalStructure
    Volume12
    Issue number5
    DOIs
    Publication statusPublished - May 2004

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