Jha, Vikash; Louis, Sherif; Chelikani, Prashen; Carpena, Xavi; Donald, Lynda J. et al. (2011). Modulation of Heme Orientation and Binding by a Single Residue in Catalase HPII of Escherichia coli. Biochemistry 50(12) , 2101-2110. 10.1021/bi200027v. [PDB: 3p9p, 3p9q, 3p9r, 3p9s, 3pq2, 3pq3, 3pq4, 3pq5, 3pq6, 3pq7, 3pq8] |
CMCF-ID |
Peer-Reviewed Article |
Health |
Herold, J. Martin; Wigle, Tim J.; Norris, Jacqueline L.; Lam, Robert; Korboukh, Victoria K. et al. (2011). Small-Molecule Ligands of Methyl-Lysine Binding Proteins. Journal of Medicinal Chemistry 54(7) , 2504-2511. 10.1021/jm200045v. [PDB: 3p8h] |
CMCF-ID |
Peer-Reviewed Article |
Health |
Shi, Rong; McDonald, Laura; Cui, Qizhi; Matte, Allan; Cygler, Miroslaw et al. (2011). Structural and mechanistic insight into covalent substrate binding by
Escherichia coli
dihydroxyacetone kinase. Proceedings of the National Academy of Sciences of the United States of America 108(4) , 1302-1307. 10.1073/pnas.1012596108. [PDB: 3pnm, 3pno, 3pnq] |
CMCF-ID |
Peer-Reviewed Article |
Health |
Lewis, Melissa; Meza-Avina, Maria Elena; Wei, Lianhu; Crandall, Ian E.; Bello, Angelica Mara et al. (2011). Novel Interactions of Fluorinated Nucleotide Derivatives Targeting Orotidine 5′-Monophosphate Decarboxylase. Journal of Medicinal Chemistry 54(8) , 2891-2901. 10.1021/jm101642g. [PDB: 3mo7] |
CMCF-ID |
Peer-Reviewed Article |
Health |
Chen; Jian An (2011). Structure-function relationship study of a loop structure in allosteric behaviour and substrate inhibition of Lactococcus lactis prolidase. Supervisor: Tanaka, Takuji. SK, Canada: University of Saskatchewan. http://hdl.handle.net/10388/etd-02252011-095142. |
CMCF-ID |
Masters Thesis |
|
Roberts, Joseph N. (2011). Identification and characterization of DyP peroxidases from Rhodococcus jostii RHA1. Supervisor: Eltis, Lindsay. British Columbia, Canada: University of British Columbia. http://hdl.handle.net/2429/31830. |
CMCF-ID |
Masters Thesis |
Materials |
El Bakkouri, M.; Pai, E.F.; Houry, W.A. (2011). Linkage between the Bacterial Acid Stress and Stringent Responses: The Structure of the Inducible Lysine Decarboxylase. Protein Data Bank: 3q16. |
CMCF-ID |
PDB Deposition |
Health |
Thede, G.L.; Edwards, R.A.; Glover, J.N.M. (2011). Structure of the periplasmic stress response protein CpxP. Protein Data Bank: 3qzc. |
CMCF-ID |
PDB Deposition |
Agriculture |
Calmettes, C.; Moraes, T.F. (2011). The crystal structures of porcine pathogen AsH57_TbpB. Protein Data Bank: 3pqu. |
CMCF-ID |
PDB Deposition |
Health |
Cygler, M.; Grishin, A.M.; Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (2011). The Phenylacetyl-CoA monooxygenase PaaAC subcomplex with acetyl-CoA. Protein Data Bank: 3pw8. |
CMCF-ID |
PDB Deposition |
Agriculture |
Cygler, M.; Grishin, A.M.; Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (2011). The Phenylacetyl-CoA monooxygenase PaaAC subcomplex with phenylacetyl-CoA. Protein Data Bank: 3pw1. |
CMCF-ID |
PDB Deposition |
Agriculture |
Gregg, K.J.; Zandberg, W.F.; Hehemann, J.-H.; Whitworth, G.E.; Deng, L.E. et al. (2011). Analysis of a new family of widely distributed metal-independent alpha mannosidases provides unique insight into the processing of N-linked glycans, Clostridium perfringens CPE0426 complexed with alpha-1,6-linked 1-thio-alpha-mannobiose. Protein Data Bank: 3qt9. |
CMCF-ID |
PDB Deposition |
Health |
Cygler, M.; Grishin, A.M.; Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (2011). The Phenylacetyl-CoA monooxygenase PaaAC subcomplex. Protein Data Bank: 3pwq. |
CMCF-ID |
PDB Deposition |
Agriculture |
Bacik, J.P.; Martin, D.R.; Mark, B.L. (2011). Crystal structure of pseudomonas aeruginosa 1,6-anhydro-n-actetylmuramic acid kinase (ANMK) bound to adenosine diphosphate. Protein Data Bank: 3qbw. |
CMCF-ID |
PDB Deposition |
Agriculture |
Bacik, J.P.; Martin, D.R.; Mark, B.L. (2011). Crystal structure of pseudomonas aeruginosa 1,6-anhydro-n-actetylmuramic acid kinase (ANMK) bound to 1,6-anhydro-n-actetylmuramic acid. Protein Data Bank: 3qbx. |
CMCF-ID |
PDB Deposition |
Agriculture |