3k7d | pdb_00003k7d

C-terminal (adenylylation) domain of E.coli Glutamine Synthetase Adenylyltransferase

spinqualitylabelsall models 3k7d, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3k7d is a 2 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. Ligands: SO4 Related: 1v4a Gene: b3053, glnE, JW3025 ("Bacillus coli" Migula 1895) 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 The X-ray structure of the C-terminal fragment, containing residues 449-946, of Escherichia coli glutamine synthetase adenylyl transferase (ATase) has been determined. ATase is part of the cascade that regulates the enzymatic activity of E. coli glutamine synthetase, a key component of the cell's machinery for the uptake of ammonia. It has two enzymatic activities, adenylyl removase (AR) and adenylyl transferase (AT), which are located in distinct catalytic domains that are separated by a regulatory (R) domain. We previously reported the three-dimensional structure of the AR domain (residues 1-440). The present structure contains both the R and AT domains. AR and AT share 24% sequence identity and also contain the beta-polymerase motif that is characteristic of many nucleotidylyl transferase enzymes. The structures overlap with an rmsd of 2.4 A when the superhelical R domain is omitted. A model for the complete ATase molecule is proposed, along with some refinements of domain boundaries. A rather more speculative model for the complex of ATase with glutamine synthetase and the nitrogen signal transduction protein PII is also presented. Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: evidence for gene duplication and evolution of a new active site.,Xu Y, Carr PD, Vasudevan SG, Ollis DL J Mol Biol. 2010 Feb 26;396(3):773-84. Epub 2009 Dec 21. PMID:20026075 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA