1v4a | pdb_00001v4a

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

spinqualitylabelsall models 1v4a, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1v4a is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Activity: [Glutamate--ammonia-ligase_adenylyltransferase [Glutamate--ammonia-ligase] adenylyltransferase], with EC number 2.7.7.42 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLNE_ECOLI] Adenylation and deadenylation of glutamate--ammonia ligase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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