Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis.
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Tadhg P Begley | Benjamin Philmus | T. Begley | S. Ealick | M. K. Fenwick | Steven E Ealick | B. Philmus | Michael K Fenwick
[1] Molecular architecture of TylM1 from Streptomyces fradiae: an N,N-dimethyltransferase involved in the production of dTDP-D-mycaminose. , 2011, Biochemistry.
[2] A. Bacher,et al. Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis , 1997, Journal of bacteriology.
[3] J. Ham,et al. Burkholderia glumae: next major pathogen of rice? , 2011, Molecular plant pathology.
[4] R. Blumenthal,et al. 1 Protein Methyltransferases: Their Distribution Among the Five Structural Classes of AdoMet-Dependent Methyltransferases. , 2006, The Enzymes.
[5] B. Levenberg,et al. On the biosynthesis of toxoflavin, an azapteridine antibiotic produced by Pseudomonas cocovenenans. , 1966, Journal of Biological Chemistry.
[6] D. Stammers,et al. GTP Cyclohydrolase II Structure and Mechanism* , 2005, Journal of Biological Chemistry.
[7] I. Hwang,et al. Structural and Functional Analysis of Phytotoxin Toxoflavin-Degrading Enzyme , 2011, PloS one.
[8] Jennifer L. Martin,et al. SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. , 2002, Current opinion in structural biology.
[9] R. Blumenthal,et al. Many paths to methyltransfer: a chronicle of convergence. , 2003, Trends in biochemical sciences.
[10] Hyun-Ju Kim,et al. ToxB encodes a canonical GTP cyclohydrolase II in toxoflavin biosynthesis and ribA expression restored toxoflavin production in a ΔtoxB mutant , 2015, Journal of the Korean Society for Applied Biological Chemistry.
[11] H. Fujii,et al. Pathogenic Bacterium Causing Seedling Rot of Rice , 1976 .
[12] L. Pearl,et al. Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase , 2007, The EMBO journal.
[13] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[14] S. Cusack,et al. Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl‐transferase , 2007, The EMBO journal.
[15] C. Lima,et al. Structure and mechanism of mRNA cap (guanine-N7) methyltransferase. , 2004, Molecular cell.
[16] Yafei Huang,et al. Catalytic mechanism of glycine N-methyltransferase. , 2003, Biochemistry.
[17] Dino Moras,et al. Functional insights from structures of coactivator‐associated arginine methyltransferase 1 domains , 2007, The EMBO journal.
[18] Nathaniel Echols,et al. The Phenix software for automated determination of macromolecular structures. , 2011, Methods.
[19] George M Sheldrick,et al. Substructure solution with SHELXD. , 2002, Acta crystallographica. Section D, Biological crystallography.
[20] Hiroaki Suga,et al. Quorum sensing and the LysR‐type transcriptional activator ToxR regulate toxoflavin biosynthesis and transport in Burkholderia glumae , 2004, Molecular microbiology.
[21] D. Groth,et al. Burkholderia glumae and B. gladioli Cause Bacterial Panicle Blight in Rice in the Southern United States. , 2009, Plant disease.
[22] A. Bacher,et al. Biosynthesis of vitamin b2 (riboflavin). , 2000, Annual review of nutrition.
[23] Jay Painter,et al. Electronic Reprint Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Motion Biological Crystallography Optimal Description of a Protein Structure in Terms of Multiple Groups Undergoing Tls Motion , 2005 .
[24] J. Qin,et al. Biochemical Control of CARM1 Enzymatic Activity by Phosphorylation* , 2009, The Journal of Biological Chemistry.
[25] A. S. Hellendoorn,et al. On the structure of toxoflavin , 2010 .
[26] W. Eisenreich,et al. Biosynthesis of riboflavin. , 2001, Vitamins and hormones.
[27] Complete Genome Sequence of Burkholderia glumae BGR1 , 2009, Journal of bacteriology.
[28] W. Berends,et al. On the origin of the toxicity of toxoflavin. , 1961, Biochimica et biophysica acta.
[29] A. G. Veen,et al. On the isolation of a toxic bacterial pigment (provisional communication). , 1933 .
[30] T. Begley,et al. Identification of the product of toxoflavin lyase: degradation via a Baeyer-Villiger oxidation. , 2012, Journal of the American Chemical Society.
[31] S. Shuman,et al. Mutational analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase reveals essential contributions of the N-terminal peptide that closes over the active site. , 2008, RNA.
[32] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[33] Y. Koiso,et al. Toxins produced by Pseudomonas glumae. , 1989 .
[34] Fumihiko Suzuki,et al. Molecular characterization of the tox operon involved in toxoflavin biosynthesis of Burkholderia glumae , 2004, Journal of General Plant Pathology.
[35] T. Black. An improved, large-scale synthesis of xanthothricin and reumycin† , 1987 .
[36] Z. Otwinowski,et al. Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[37] I. Yamaguchi,et al. Toxoflavin is an Essential Factor for Virulence of Burkholderia glumae Causing Rice Seedling Rot Disease , 1998 .
[38] G. Brown,et al. Purification and properties of guanosine triphosphate cyclohydrolase II from Escherichia coli. , 1975, The Journal of biological chemistry.
[39] J. Kostan,et al. Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis. , 2014, Acta crystallographica. Section D, Biological crystallography.
[40] Yuan-Chih Chang,et al. Crystal Structure of a Bifunctional Deaminase and Reductase from Bacillus subtilis Involved in Riboflavin Biosynthesis* , 2006, Journal of Biological Chemistry.
[41] G. Brown,et al. Presence of Escherichia coli of a deaminase and a reductase involved in biosynthesis of riboflavin , 1978, Journal of bacteriology.
[42] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[43] K. Iiyama,et al. A role of phytotoxin in virulence of Pseudomonas glumae Kurita et Tabei , 1995 .
[44] T. Begley,et al. Toxoflavin lyase requires a novel 1-His-2-carboxylate facial triad. , 2011, Biochemistry.
[45] K. Henrick,et al. Inference of macromolecular assemblies from crystalline state. , 2007, Journal of molecular biology.
[46] G. Sheldrick. A short history of SHELX. , 2008, Acta crystallographica. Section A, Foundations of crystallography.
[47] P. Nordlund,et al. The crystal structure of the bifunctional deaminase/reductase RibD of the riboflavin biosynthetic pathway in Escherichia coli: implications for the reductive mechanism. , 2007, Journal of molecular biology.
[48] Tadhg P Begley,et al. Investigations into the Biosynthesis, Regulation, and Self‐Resistance of Toxoflavin in Pseudomonas protegens Pf‐5 , 2015, Chembiochem : a European journal of chemical biology.
[49] J. Montgomery,et al. The preparation of pyrimido[5,4‐e]‐as‐Triazine‐5,7(6H,8H)‐dione , 1968 .
[50] Liisa Holm,et al. Dali server: conservation mapping in 3D , 2010, Nucleic Acids Res..
[51] P. Damme,et al. On toxoflavin, the yellow poison of pseudomonas cocovenenans , 2010 .
[52] Ingyu Hwang,et al. Toxoflavin Produced by Burkholderia glumae Causing Rice Grain Rot Is Responsible for Inducing Bacterial Wilt in Many Field Crops. , 2003, Plant disease.
[53] A. Bacher,et al. Biosynthesis of riboflavin: cloning, sequencing, mapping, and expression of the gene coding for GTP cyclohydrolase II in Escherichia coli , 1993, Journal of bacteriology.
[54] Alexei Vagin,et al. Molecular replacement with MOLREP. , 2010, Acta crystallographica. Section D, Biological crystallography.