1v4a: Difference between revisions

Revision as of 15:56, 28 July 2008

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File:1v4a.png

Template:STRUCTURE 1v4a

Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferaseStructure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase

Template:ABSTRACT PUBMED 15130478

About this StructureAbout this Structure

1V4A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase'''
+===Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase===
-==Overview==
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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 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.
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