Kuatsjah, Eugene; Chan, Anson C.K.; Kobylarz, Marek J.; Murphy, Michael E.P.; Eltis, Lindsay D. et al. (2017). The bacterial meta-cleavage hydrolase LigY belongs to the amidohydrolase superfamily, not to the α/β-hydrolase superfamily. Journal of Biological Chemistry 292(44) , 18290-18302. 10.1074/jbc.m117.797696. [PDB: 5vn5] |
CMCF-BM |
Peer-Reviewed Article |
Health |
Krishnamurthy, H.; Zhuang, N.; Qiang, D.; Wu, Y.; Klein, D.J. et al. (2024). Structure of SARS-Cov2 3CLPro in complex with Compound 27. Protein Data Bank: 8ute. |
CMCF-BM |
PDB Deposition |
Health |
Kolesnikov; Maxim (2018). Characterisation of substrate preference in staphylococcus aureus siderophore biosynthesis. Supervisor: Murphy, Michael. British Columbia, Canada: University of British Columbia. http://hdl.handle.net/2429/67142. |
CMCF-BM |
Masters Thesis |
Health |
Kobylarz, M.J.; Heieis, G.A.; Loutet, S.A.; Murphy, M.E.P. (2017). Oxidoreductase IruO in the reduced form. Protein Data Bank: 5twb. |
CMCF-BM |
PDB Deposition |
Health |
Kobylarz; Marek John (2016). Siderophore-mediated iron metabolism in Staphylococcus aureus. Supervisor: Murphy, Michael. British Columbia, Canada: University of British Columbia. http://hdl.handle.net/2429/57023. |
CMCF-BM |
Doctoral Thesis |
Health |
Kobylarz, Marek J.; Heieis, Graham A.; Loutet, Slade A.; Murphy, Michael E. P. (2017). Iron Uptake Oxidoreductase (IruO) Uses a Flavin Adenine Dinucleotide Semiquinone Intermediate for Iron-Siderophore Reduction. ACS Chemical Biology 12(7) , 1778-1786. 10.1021/acschembio.7b00203. [PDB: 5twb] |
CMCF-BM |
Peer-Reviewed Article |
Health |
Kobylarz, Marek J.; Grigg, Jason C.; Liu, Yunan; Lee, Mathew S. F.; Heinrichs, David E. et al. (2016). Deciphering the Substrate Specificity of SbnA, the Enzyme Catalyzing the First Step in Staphyloferrin B Biosynthesis. Biochemistry 55(6) , 927-939. 10.1021/acs.biochem.5b01045. [PDB: 5d84] |
CMCF-BM, CMCF-ID |
Peer-Reviewed Article |
Health |
King, Dustin T.; Worrall, Liam J.; Gruninger, Robert; Strynadka, Natalie C. J. (2012). New Delhi Metallo-β-Lactamase: Structural Insights into β-Lactam Recognition and Inhibition. Journal of the American Chemical Society 134(28) , 11362-11365. 10.1021/ja303579d. [PDB: 4exy, 4ey2, 4eyb, 4eyf, 4eyl] |
CMCF-BM, CMCF-ID |
Peer-Reviewed Article |
Health |
King, Dustin T.; Lameignere, Emilie; Strynadka, Natalie C.J. (2014). Structural Insights into the Lipoprotein Outer Membrane Regulator of Penicillin-binding Protein 1B. Journal of Biological Chemistry 289(27) , 19245-19253. 10.1074/jbc.m114.565879. [PDB: 4q6l, 4q6v, 4q6z] |
CMCF-BM |
Peer-Reviewed Article |
Health |
King, Dustin T.; King, Andrew M.; Lal, Sarah M.; Wright, Gerard D.; Strynadka, Natalie C. J. et al. (2015). Molecular Mechanism of Avibactam-Mediated β-Lactamase Inhibition. ACS Infectious Diseases 1(4) , 175-184. 10.1021/acsinfecdis.5b00007. [PDB: 4s2i, 4s2j, 4s2k, 4s2n, 4s2o, 4s2p] |
CMCF-BM |
Peer-Reviewed Article |
Health |
King, D.T.; Strynadka, N.C.J. (2015). OXA-48 in complex with Avibactam at pH 6.5. Protein Data Bank: 4s2j. |
CMCF-BM |
PDB Deposition |
Health |
King, D.T.; Strynadka, N.C.J. (2015). OXA-10 in complex with Avibactam. Protein Data Bank: 4s2o. |
CMCF-BM |
PDB Deposition |
Health |
King, D.T.; Strynadka, N.C.J. (2015). CTX-M-15 in complex with Avibactam. Protein Data Bank: 4s2i. |
CMCF-BM |
PDB Deposition |
Health |
King, D.T.; Strynadka, N.C.J. (2015). OXA-48 in complex with Avibactam at pH 8.5. Protein Data Bank: 4s2n. |
CMCF-BM |
PDB Deposition |
Health |
King, D.T.; Strynadka, N.C.J. (2015). OXA-48 in complex with Avibactam at pH 7.5. Protein Data Bank: 4s2k. |
CMCF-BM |
PDB Deposition |
Health |