1v4a
From Proteopedia
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Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase
Overview
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 residues that are conserved in, polbeta-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.
About this Structure
1V4A is a Single protein structure of sequence from Escherichia coli. Active as [Glutamate--ammonia-ligase_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number 2.7.7.42 Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase., Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL, Structure. 2004 May;12(5):861-9. PMID:15130478[[Category: [Glutamate--ammonia-ligase] adenylyltransferase]]
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