3CES

Crystal Structure of E.coli MnmG (GidA), a Highly-Conserved tRNA Modifying Enzyme

Summary for 3CES

• Entry DOI: 10.2210/pdb3ces/pdb
• Descriptor: tRNA uridine 5-carboxymethylaminomethyl modification enzyme gidA (2 entities in total)
• Functional Keywords: trna modification, fad binding domain, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, rna binding protein
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6U3
• Total number of polymer chains: 4
• Total formula weight: 288203.06

Authors

Shi, R.,Matte, A.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2008-02-29, release date: 2009-03-03, Last modification date: 2024-02-21)

Primary citation

Shi, R.,Villarroya, M.,Ruiz-Partida, R.,Li, Y.,Proteau, A.,Prado, S.,Moukadiri, I.,Benitez-Paez, A.,Lomas, R.,Wagner, J.,Matte, A.,Velazquez-Campoy, A.,Armengod, M.E.,Cygler, M.
Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
J.Bacteriol., 191:7614-7619, 2009

PubMed Abstract: The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.

PubMed: 19801413
DOI: 10.1128/JB.00650-09

Experimental method

X-RAY DIFFRACTION (2.412 Å)