Broken-Symmetry DFT Computations for the Reaction Pathway of IspH, an Iron–Sulfur Enzyme in Pathogenic Bacteria

Autor: Louis Noodleman, Debra Ann Giammona, Patrick G. Blachly, Donald Bashford, Gregory M. Sandala, J. Andrew McCammon

Publikováno v: Blachly, PG; Sandala, GM; Giammona, DA; Bashford, D; McCammon, JA; & Noodleman, L. (2015). Broken-Symmetry DFT Computations for the Reaction Pathway of IspH, an Iron-Sulfur Enzyme in Pathogenic Bacteria. Inorganic Chemistry, 54(13), 6439-6461. doi: 10.1021/acs.inorgchem.5b00751. UC San Diego: Retrieved from: http://www.escholarship.org/uc/item/3h00n5j3
Inorganic Chemistry
Inorganic chemistry, vol 54, iss 13

The recently discovered methylerythritol phosphate (MEP) pathway provides new targets for the development of antibacterial and antimalarial drugs. In the final step of the MEP pathway, the [4Fe–4S] IspH protein catalyzes the 2e–/2H+ reductive deh

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https://doi.org/10.1021/acs.inorgchem.5b00751

Monitoring ligand-induced protein ordering in drug discovery

Autor: Jaeki Min, Kristin Finch, Richard W. Kriwacki, Michael A. Dyer, David Ban, Lie Min, R. Kiplin Guy, Lyra Griffiths, Christy R. Grace, Nagakumar Bharatham, Anand Mayasundari, Donald Bashford

While the gene for p53 is mutated in many human cancers causing loss of function, many others maintain a wild-type gene but exhibit reduced p53 tumor suppressor activity through overexpression of the negative regulators, Mdm2 and/or MdmX. For the lat

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https://europepmc.org/articles/PMC4826315/

Analysis of the Active-Site Mechanism of Tyrosyl-DNA Phosphodiesterase I: A Member of the Phospholipase D Superfamily

Autor: Stephen W. White, Nauzanene Jafari, Donald Bashford, Robert C.A.M. van Waardenburg, Stefan Gajewski, Nagakumar Bharatham, Evan Q. Comeaux

Publikováno v: Journal of Molecular Biology. 415:741-758

Tyrosyl-DNA phosphodiesterase I (Tdp1) is a member of the phospholipase D superfamily that hydrolyzes 3′-phospho-DNA adducts via two conserved catalytic histidines—one acting as the lead nucleophile and the second acting as a general acid/base. S

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0519bcdfc27ee5fb0f85f4efd2d54dfd
https://doi.org/10.1016/j.jmb.2011.11.044

A Fluid Salt-bridging Cluster and the Stabilization of p53

Autor: Jason J. Durant, Thu Zar Lwin, Donald Bashford

Publikováno v: Journal of Molecular Biology. 373:1334-1347

p53 is a homotetrameric tumor suppressor protein that is found to be mutated in most human cancers. Some of these mutations, particularly mutations to R337, fall in the tetramerization domain and cause defects in tetramer formation leading to loss of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72e3db1c0af5bc69d662dbf6f749771c
https://doi.org/10.1016/j.jmb.2007.07.080

On the Role of the Conserved Aspartate in the Hydrolysis of the Phosphocysteine Intermediate of the Low Molecular Weight Tyrosine Phosphatase

Autor: Dilip Asthagiri, Louis Noodleman, Donald Bashford, Tiqing Liu, Robert L. Van Etten

Publikováno v: Journal of the American Chemical Society. 126:12677-12684

The usual rate-determining step in the catalytic mechanism of the low molecular weight tyrosine phosphatases involves the hydrolysis of a phosphocysteine intermediate. To explain this hydrolysis, general base-catalyzed attack of water by the anion of

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https://doi.org/10.1021/ja048638o