3G05

Crystal structure of N-terminal domain (2-550) of E.coli MnmG

Summary for 3G05

• Entry DOI: 10.2210/pdb3g05/pdb
• Related: 3CES
• Descriptor: tRNA uridine 5-carboxymethylaminomethyl modification enzyme mnmG, SULFATE ION (2 entities in total)
• Functional Keywords: trna-modification enzyme, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, fad, flavoprotein, nad, trna processing, rna binding protein
• Biological source: Escherichia coli O157:H7 EDL933
• Cellular location: Cytoplasm : Q8XAY0
• Total number of polymer chains: 2
• Total formula weight: 128282.63

Authors

Shi, R.,Matte, A.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2009-01-27, release date: 2009-10-20, Last modification date: 2023-09-06)

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 (3.49 Å)