1V4A

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

Summary for 1V4A

• Entry DOI: 10.2210/pdb1v4a/pdb
• Descriptor: Glutamate-ammonia-ligase adenylyltransferase (2 entities in total)
• Functional Keywords: main alpha helix, dna polymerase beta motif, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 51037.91

Authors

Xu, Y.,Zhang, R.,Joachimiak, A.,Carr, P.D.,Ollis, D.L.,Vasudevan, S.G. (deposition date: 2003-11-12, release date: 2004-07-27, Last modification date: 2023-12-27)

Primary citation

Xu, Y.,Zhang, R.,Joachimiak, A.,Carr, P.D.,Huber, T.,Vasudevan, S.G.,Ollis, D.L.
Structure of the n-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase
Structure, 12:861-869, 2004

PubMed 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 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.

PubMed: 15130478
DOI: 10.1016/j.str.2004.02.029

Experimental method

X-RAY DIFFRACTION (2 Å)