Crystal structure of Staphylococcus aureus Zn-glyoxalase I: new subfamily of glyoxalase I family

References

• Altschul, S. F. , Madden, T. L. , Schäffer, A. A. , Zhang, J. , Zhang, Z. , Miller, W. , & Lipman, D. J. (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Research , 25 , 3389–3402.10.1093/nar/25.17.3389
   PubMed Web of Science ®Google Scholar
• Arai, M. , Nihonmatsu-Kikuchi, N. , Itokawa, M. , Rabbani, N. , & Thornalley, P. J. (2014). Measurement of glyoxalase activities. Biochemical Society Transactions , 42 , 491–494.10.1042/BST20140010
   PubMedGoogle Scholar
• Aronsson, A. C. , Marmstal, E. , & Mannervik, B. (1978). Glyoxalase I, a zinc metalloenzyme of mammals and yeast. Biochemical and Biophysical Research Communications , 81 , 1235–1240.10.1016/0006-291X(78)91268-8
   PubMed Web of Science ®Google Scholar
• Ayoub, F. M. , Allen, R. E. , & Thornalley, P. J. (1993). Inhibition of proliferation of human leukemia 60 cells by methylglyoxal in vitro . Leukemia Research , 17 , 397–401.10.1016/0145-2126(93)90094-2
   PubMed Web of Science ®Google Scholar
• Bricogne, G. , Blanc, E. , Brandl, M. , Flensburg, C. , Keller, P. , Paciorek, W. , … Womack, T. O. (2011). BUSTER (Version 2.10.0, Ed.) . Cambridge: Global Phasing Ltd.
   Google Scholar
• Cameron, A. D. , Olin, B. , Ridderstrom, M. , Mannervik, B. , & Jones, T. A. (1997). Crystal structure of human glyoxalase I – Evidence for gene duplication and 3D domain swapping. The EMBO Journal , 16 , 3386–3395.10.1093/emboj/16.12.3386
   PubMed Web of Science ®Google Scholar
• Clugston, S. L. , Barnard, J. F. J. , Kinach, R. , Miedema, D. , Ruman, R. , Daub, E. , & Honek, J. F. (1998). Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: Evidence for optimal activation by nickel ions. Biochemistry , 37 , 8754–8763.10.1021/bi972791w
   PubMed Web of Science ®Google Scholar
• Dumas, P. , Bergdoll, M. , Cagnon, C. , & Masson, J. M. (1994). Crystal structure and site-directed mutagenesis of a bleomycin resistance protein and their significance for drug sequestering. The EMBO Journal , 13 , 2483–2492.
   PubMed Web of Science ®Google Scholar
• Emsley, P. , Lohkamp, B. , Scott, W. G. , & Cowtan, K. (2010). Features and development of Coot. Acta Crystallographica , D66 , 486–501.
   Google Scholar
• Evans, P. R. (2006). Scaling and assessment of data quality. Acta Crystallographica , D62 , 72–82.
   Google Scholar
• Evans, P. R. (2011). An introduction to data reduction: Space-group determination, scaling and intensity statistics. Acta Crystallographica , D67 , 282–292.
   Google Scholar
• Evans, P. R. , & Murshudov, G. N. (2013). How good are my data and what is the resolution? Acta Crystallographica , D69 , 1204–1214.
   Google Scholar
• Fielding, A. J. , Kovaleva, E. G. , Farquhar, E. R. , Lipscomb, J. D. , & Que, L. (2011). A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenase. JBIC Journal of Biological Inorganic Chemistry , 16 , 341–355.10.1007/s00775-010-0732-0
   PubMed Web of Science ®Google Scholar
• He, M. M. , Clugston, S. L. , Honek, J. F. , & Matthews, B. W. (2000). Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry , 39 , 8719–8727.10.1021/bi000856g
   PubMed Web of Science ®Google Scholar
• Kabsch, W. (2010). XDS. Acta Crystallographica , D66 , 125–132.
   Google Scholar
• Lam, R. , Chan, T. , Battaile, K. P. , Mihajlovic, V. , Romanov, V. , Soloveychik, M. , … Chirgadze, N. Y. (2010). Crystal structure of a hypothethical protein from Staphylococcus aureus . RCSB PDB, PDB ID: 3L20.
   Google Scholar
• Langer, G. , Cohen, S. X. , Lamzin, V. S. , & Perrakis, A. (2008). Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nature Protocols , 3 , 1171–1179.10.1038/nprot.2008.91
   PubMed Web of Science ®Google Scholar
• McCarthy, A. A. , Baker, H. M. , Shewry, S. C. , Patchett, M. L. , & Baker, E. N. (2001). Crystal structure of methylmalonyl-coenzyme A epimerase from P. shermanii: A novel enzymatic function on an ancient metal binding scaffold. Structure , 9 , 637–646.10.1016/S0969-2126(01)00622-0
   PubMed Web of Science ®Google Scholar
• Murshudov, G. N. , Vagin, A. A. , & Dodson, E. J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallographica , D53 , 240–255.
   Google Scholar
• Santarius, T. , Bignell, G. R. , Greenman, C. D. , Widaa, S. , Chen, L. , Mahoney, C. L. , … Stratton, M. R. (2010). GLO1 – A novel amplified gene in human cancer. Genes, Chromosomes & Cancer , 49 , 711–725.10.1002/gcc.20784
   PubMed Web of Science ®Google Scholar
• Sellin, S. , Eriksson, L. E. G. , Aronsson, A. C. , & Mannervik, B. (1983). Octahedral metal coordination in the active site of glyoxalase I as evidenced by the properties of Co(II)-glyoxalase I. Journal of Biological Chemistry , 258 , 2091–2093.
   PubMed Web of Science ®Google Scholar
• Sellin, S. , & Mannervik, B. (1984). Metal dissociation constants for glyoxalase I reconstituted with Zn2+, Co2+, Mn2+, and Mg2+ . Journal of Biological Chemistry , 259 , 11426–11429.
   PubMed Web of Science ®Google Scholar
• Suttisansanee, U. , Lau, K. , Lagishetty, S. , Rao, K. N. , Swaminathan, S. , Sauder, J. M. , … Honek, J. F. (2011). Structural variation in bacterial glyoxalase I enzymes: Investigation of the metalloenzyme glyoxalase I from clostridium acetobutylicum. Journal of Biological Chemistry , 286 , 38367–38374.10.1074/jbc.M111.251603
   PubMed Web of Science ®Google Scholar
• Thornalley, P. J. (1996). Pharmacology of methylglyoxal: Formation, modification of proteins and nucleic acids, and enzymatic detoxigfication – A role in pathogenesis and antiproliferative chemotherapy. General Pharmacology: The Vascular System , 27 , 565–573.10.1016/0306-3623(95)02054-3
   PubMedGoogle Scholar
• Thornalley, P. J. (2003). Glyaxalase I – Structure, function and critical role in the enzymatic defence against glycation. Biochemical Society Transactions , 31 , 1343–1348.10.1042/bst0311343
   PubMed Web of Science ®Google Scholar
• Vander Jagt, D. L. (1989). The glyoxalase system . In D. Dolphin , R. Poulson , & O. Avramovic (Eds.), Glutathione: Chemical, biochemical and medical aspects. Part A (pp. 597–641). New York, NY: Wiley.
   Google Scholar
• Vonrhein, C. , Blanc, E. , Roversi, P. , & Bricogne, G. (2007). Automated structure solution with autoSHARP. Methods in Molecular Biology , 364 , 215–230.
   PubMedGoogle Scholar
• Vonrhein, C. , Flensburg, C. , Keller, P. , Sharff, A. , Smart, O. , Paciorek, W. , … Bricogne, G. (2011). Data processing and analysis with the autoPROC toolbox. Acta Crystallographica , D67 , 293–302.
   Google Scholar
• Wallace, A. C. , Laskowski, R. A. , & Thornton, J. M. (1996). LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions. Protein Engineering , 8 , 127–134.
   Google Scholar
• Winn, M. D. , Ballard, C. C. , Cowtan, K. D. , Dodson, E. J. , Emsley, P. , Evans, P. R. , … Wilson, K. S. (2011). Overview of the CCP4 suite and current developments. Acta Crystallographica , D67 , 235–242.
   Google Scholar