Oakley, Dr Aaron J. BSc Tasmania PhD St Vincent’s IMR Melbourne - Structural Biology
 


2008

Board PG, Coggan M, Cappello J, Zhou H, Oakley AJ, Anders MW S-(4-Nitrophenacyl)glutathione is a specific substrate for glutathione transferase omega 1-1. Anal. Biochem. (2008), 374(1), 25-30. http://dx.doi.org/10.1016/j.ab.2007.09.029
 

Jackson CJ, Hadler KS, Carr PD, Oakley AJ, Yip S, Schenk G, Ollis DL Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. (2008), 64(8), 681-685. http://dx.doi.org/10.1107/S1744309108017600
 

Oakley AJ, Yamada T, Liu D, Coggan M, Clark AG, Board PG The identification and structural characterization of C7orf24 as γ-glutamyl cyclotransferase: an essential enzyme in the γ-glutamyl cycle. J. Biol. Chem. (2008), 283(32), 22031-22042. http://dx.doi.org/10.1074/jbc.M803623200 [Erratum: J. Biol. Chem. (2008), 283(46), 32152.]
 

Paiva L, Marcos R, Creus A, Coggan M, Oakley AJ, Board PG Polymorphism of glutathione transferase Omega 1 in a population exposed to a high environmental arsenic burden. Pharmacogenet. Genomics (2008), 18(1), 1-10. http://dx.doi.org/10.1097/FPC.0b013e3282f29663
 

2007

Burden CJ, Oakley AJ Anisotropic atomic motions in high-resolution protein crystallography molecular dynamics simulations. Phys. Biol. (2007), 4(2), 79-90. http://dx.doi.org/10.1088/1478-3975/4/2/002
 

Qi R, Fetzner S, Oakley AJ Crystallization and diffraction data of 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase: a cofactor-free oxygenase of the α/β-hydrolase family. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. (2007), 63(5), 378-381. http://dx.doi.org/10.1107/S1744309107013760
 

2006

Hughes J L, Razeghifard R, Logue M, Oakley A, Wydrzynski T, Krausz E Magneto-Optic Spectroscopy of a Protein Tetramer Binding Two Exciton-Coupled Chlorophylls. J Am. Chem. Soc. (2006), 128(11), 3649-3658.http://dx.doi.org/10.1021/ja056576b
 

Mulcair M D, Schaeffer P M, Oakley A J, Cross H F, Neylon C, Hill T M, Dixon N E A molecular mousetrap determines polarity of termination of DNA replication in E. coli. Cell (2006), 125(7), 1309-1319. http://dx.doi.org/10.1016/j.cell.2006.04.040
 

O'Mara M, Oakley A, Bröer, S Mechanism and putative structure of B0-like neutral amino acid transporters. J. Membrane Biol. (2006), 213(2), 111-118. http://dx.doi.org/10.1007/s00232-006-0879-3
 

2005

Bourgault, R., Oakley, A.J., Bewley, J.D., Wilce, M.C.J. Three-dimensional structure of (1,4)-β-D-mannan mannanohydrolase from tomato fruit. Protein Sci. (2005), 14(5), 1233-1241. http://dx.doi.org/10.1110/ps.041260905
 

Oakley, A.J. Glutathione transferases: new functions. Curr. Opin. Struct. Biol. (2005), 15(6), 716-723. http://dx.doi.org/10.1016/j.sbi.2005.10.005
 

Oakley, A.J., Loscha, K.V., Schaeffer, P.M., Liepinsh, E., Pintacuda, G., Wilce, M.C.J., Otting, G., Dixon, N.E. Crystal and solution structures of the helicase-binding domain of Escherichia coli primase. J. Biol. Chem. (2005), 280(12), 11495-11504. http://dx.doi.org/10.1074/jbc.M412645200
 

Schmidberger, J.W., Oakley, A.J., Tsang, J.S.H., Wilce, M.C.J. Purification, crystallization and preliminary crystallographic analysis of DehIVa, a dehalogenase from Burkholderia cepacia MBA4. Acta Crystallogr., Sect. F (2005), 61(3), 271-273. http://dx.doi.org/10.1107/S1744309105002472
 

Udomsinprasert, R., Pongjaroenkit, S., Wongsantichon, J., Oakley, A.J., Prapanthadara, L., Wilce, M.C.J., Ketterman, A.J. Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme. Biochem. J. (2005), 388(3), 763-771. http://dx.doi.org/10.1042/BJ20042015
 

Watt, S.J., Oakley, A., Sheil, M.M., Beck, J.L. Comparison of negative and positive ion electrospray ionization mass spectra of calmodulin and its complex with trifluoperazine. Rapid Commun. Mass Spectrom. (2005), 19(15), 2123-2130. http://dx.doi.org/10.1002/rcm.2039
 

Webb, A.I., Dunstone, M.A., Williamson, N.A., Price, J.D., de Kauwe, A., Chen, W., Oakley, A., Perlmutter, P., McCluskey, J., Aguilar, M.-I., Rossjohn, J., Purcell, A.W. T Cell determinants incorporating β-amino acid residues are protease resistant and remain immunogenic in vivo. J. Immunol. (2005), 175(6), 3810-3818. http://www.jimmunol.org/cgi/content/abstract/175/6/3810
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2004

Bogoyevitch, M.A., Boehm, I., Oakley, A., Ketterman, A.J., Barr, R.K. Targeting the JNK MAPK cascade for inhibition: basic science and therapeutic potential. Biochim. Biophys. Acta (2004), 1697(1–2), 89–101.
 

Loscha, K., Oakley, A.J., Bancia, B., Schaeffer, P.M., Prosselkov, P., Otting, G., Wilce, M.C.J., Dixon, N.E. Expression, purification, crystallization, and NMR studies of the helicase interaction domain of Escherichia coli DnaG primase. Protein Expr. Purif. (2004), 33(2), 304–310.
 

Oakley, A.J., Klvana, M., Otyepka, M., Nagata, Y., Wilce, M.C.J., Damborsk, J. Crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 Å resolution: dynamics of catalytic residues. Biochemistry (2004), 43(4), 870–878.
 

2003

Oakley, A.J., Heinrich, T., Thompson, C.A., Wilce, M.C.J. Characterisation of a family 11 xylanase from Bacillus subtilis B230 used for paper bleaching. Acta Cryst. D (2003), 59, 627-636.
 

Oakley, A.J., Prosselkov, P., Wijffels, G., Beck, J.L., Wilce, M.C., Dixon, N.E. Flexibility revealed by the 1.85 Å crystal structure of the beta sliding-clamp subunit of Escherichia coli DNA polymerase III. Acta Cryst. D (2003), 59, 1192-1199.
 

Ortiz-Salmeron, E., Nuccetelli, M., Oakley, A.J., Parker, M.W., Lo Bello, M., Garcia-Fuentes, L. Thermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathione. J. Biol. Chem. (2003), 278, 46938-46948.
 

Petersen, J., Wilmann, P.G., Beddoe, T., Oakley, A.J., Devenish, R.J., Prescott, M., Rossjohn, J. The 2.0-Å crystal structure of eqFP611, a far red fluorescent protein from the sea anemone Entacmaea quadricolor. J. Biol. Chem. (2003), 278, 44626-44631.
 

Prescott, M., Ling, M., Beddoe, T., Oakley, A.J., Dove, S., Hoegh-Guldberg, O., Devenish, R.J., Rossjohn, J. The 2.2Å crystal structure of a pocilloporin pigment reveals a non-planar chromophore conformation. Structure (2003), 11, 275-284.
 

Streltsov, V.A., Prokop, Z., Damborsky, J., Nagata, Y., Oakley, A.J., Wilce, M.C. Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: x-ray crystallographic studies of dehalogenation of brominated substrates. Biochemistry (2003), 42, 10104-10112.
 

2002

Oakley, A.J., Prokop, Z., Bohac, M., Kmunicek, J., Jedlicka, T., Monincova, M., Kuta-Smatanova, I., Nagata, Y., Damborsky, J., Wilce, M.C.J. Exploring the structure and activity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26: evidence for product- and water-mediated inhibition. Biochemistry (2002), 41, 4847-4855.
 


2001

Oakley, A.J., Harnnoi, T., Udomsinprasert, R., Jirajaroenrat, K., Ketterman, A.J., Wilce, M.C. The crystal structures of glutathione S-transferases isozymes 1-3 and 1-4 from Anopheles dirus species B. Protein Sci. (2001), 10, 2176-2185.
 

Oakley, A.J., Jirajaroenrat, K., Harnnoi, T., Ketterman, A.J., Wilce, M.C. Crystallization of two glutathione S-transferases from an unusual gene family. Acta Cryst. D (2001), 57, 870-872.
 

Oakley, A.J., Ketterman, A., Wilce, M.C. Structural biology and its applications to the health sciences. Croat. Med. J. (2001), 42, 375-378.
 


2000

Micaloni, C., Mazzetti, A.P., Nuccetelli, M., Rossjohn, J., McKinstry, W.J., Antonini, G., Caccuri, A.M., Oakley, A.J., Federici, G., Ricci, G., Parker, M.W., Lo Bello, M. Valine 10 may act as a driver for product release from the active site of human glutathione transferase P1-1. Biochemistry (2000), 39, 15961-15970.
 

Oakley, A.J., Wilce, M.C.J. Macromolecular crystallography as a tool for investigating drug, enzyme and receptor interactions. Clin. Exp. Pharmacol. Physiol. (2000), 27, 145-151.
 

Rossjohn, J., McKinstry, W.J., Oakley, A.J., Parker, M.W., Stenberg, G., Mannervik, B., Dragani, B., Cocco, R., Aceto, A. Structures of thermolabile mutants of human glutathione transferase P1-1. J. Mol. Biol. (2000), 302, 295-302.
 


1999

Oakley, A.J., Lo Bello, M., Nuccetelli, M., Mazzetti, A.P., Parker, M.W.The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site). J. Mol. Biol. (1999), 291, 913-926.
 

Oakley, A.J., Martinac, B., Wilce, M.C. Structure and function of the bacterial mechanosensitive channel of large conductance. Protein Sci. (1999), 8, 1915-1921.
 

Oakley, A.J., Rossjohn, J., McKinstry, W.J., Flanagan, J., Board, P.G., Lo Bello, M., Ricci, G., Parker, M.W. Structure/function studies of pi and theta class glutathione transferases. Clin. Chem. Enzyme Commun. (1999), 8, 231-238.
 


1998

Lo Bello, M., Nuccetelli, M., Chiessi, E., Lahm, A., Mazzetti, A.P., Battistoni, A., Caccuri, A.M., Oakley, A.J., Parker, M.W., Tramontano, A., Federici, G., Ricci, G.Mutations of gly to ala in human glutathione transferase P1-1 affect helix 2 (G-site) and induce positive cooperativity in the binding of glutathione. J. Mol. Biol. (1998), 284, 1717-1725.
 

McKinstry, W.J., Oakley, A.J., Rossjohn, J., Verger, D., Tan, K.L., Board, P.G., Parker, M.W. Preliminary x-ray crystallographic studies of a newly defined human theta-class glutathione transferase. Acta Cryst. D (1998), 54, 148-150.
 

Nicotra, M., Paci, M., Sette, M., Oakley, A.J., Parker, M.W., Lo Bello, M., Caccuri, A.M., Federici, G., Ricci, G. Solution structure of glutathione bound to human glutathione transferase P1-1: comparison of NMR measurements with the crystal structure. Biochemistry (1998), 37, 3020-3027.
 


Oakley, A.J., Lo Bello, M., Ricci, G., Federici, G., Parker, M.W.Evidence for an induced-fit mechanism operating in pi class glutathione transferases. Biochemistry (1998), 37, 9912-9917.
 

Rossjohn, J., McKinstry, W.J., Oakley, A.J., Verger, D., Flanagan, J., Chelvanayagam, G., Tan, K.L., Board, P.G., Parker, M.W. Human theta class glutathione transferase: the crystal structure reveals a sulfate-binding pocket within a buried active site. Structure (1998), 6, 309-322.
 


1997

Oakley, A.J., Lo Bello, M., Battistoni, A., Rici, G., Rossjohn, J., Villar, H., Parker, M.W. The structures of human glutathione transferase Pl-1 in complex with glutathione and various inhibitors at high resolution. J. Mol. Biol. (1997), 274, 84-100.
 

Oakley, A.J., Lo Bello, M., Mazzetti, A.P., Federici, G., Parker, M.W. The glutathione conjugate of ethacrynic acid can bind to human pi class glutathione transferase P1-1 in two different modes. FEBS Lett. (1997), 419, 32-36.
 

Oakley, A.J., Rossjohn, J., Lo Bello, M., Caccuri, A.M., Federici, G., Parker, M.W. The three dimensional structure of the human pi class glutathione transferase Pl-1 in complex with the inhibitor ethacrynic acid and its glutathione conjugate. Biochemistry (1997), 36, 576-585.
 


1996

Lo Bello, M., Oakley, A.J., Battistoni, A., Mazzetti, A.P., Nuccetelli, M., Mazzarese, G., Rossjohn, J., Parker, M.W., Ricci, G. Site-directed mutagenesis of glutathione transferase P1-1: role of tyrosine 108 investigated by crystallographic analysis and kinetic studies of the Y108F mutant enzyme. Biochemistry (1996), 36, 6207-6217.
 

Wilce, M.C.J., Oakley, A.J., Rossjohn, J., Feil, S.C., LoBello, M., Ricci, C., Board, P.C., Parker, M.W. Crystallographic studies on pi- and theta-class glutathione s-transferases In: Glutathione S-Transferases, Structure, Function and Clinical Applications, Vermeulin, N.P.E., Mulder, C.J., Nieuwenhuyse, H., Peters, W.H.M. and van Bladeren, P.J., eds., Taylor and Francis Ltd.: London, (1996), pp 39-48.

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