1nmt
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N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A
OverviewOverview
N-myristoyl transferase (NMT) catalyzes the transfer of the fatty acid, myristate from myristoyl-CoA to the N-terminal glycine of substrate, proteins, and is found only in eukaryotic cells. The enzyme in this study, is the 451 amino acid protein produced by Candida albicans, a yeast, responsible for the majority of systemic infections in immuno-compromised, humans. NMT activity is essential for vegetative growth, and the structure, was determined in order to assist in the discovery of a selective, inhibitor of NMT which could be developed as an anti-fungal drug. NMT has, no sequence homology with other protein sequences and has a novel, alpha/beta fold which shows internal two-fold symmetry, which may be a, result of gene duplication. On one face of the protein there is a long, curved, relatively uncharged groove, at the center of which is a deep, pocket. The pocket floor is negatively charged due to the vicinity of the, C-terminal carboxylate and a nearby conserved glutamic acid residue, which, separates the pocket from a cavity. These observations, considered, alongside the positions of residues whose mutation affects substrate, binding and activity, suggest that the groove and pocket are the sites of, substrate binding and the floor of the pocket is the catalytic center.
About this StructureAbout this Structure
1NMT is a Single protein structure of sequence from Candida albicans with GOL as ligand. Active as Transferase, with EC number 2.1.3.97 Structure known Active Sites: AVE, BVE and CVE. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the anti-fungal target N-myristoyl transferase., Weston SA, Camble R, Colls J, Rosenbrock G, Taylor I, Egerton M, Tucker AD, Tunnicliffe A, Mistry A, Mancia F, de la Fortelle E, Irwin J, Bricogne G, Pauptit RA, Nat Struct Biol. 1998 Mar;5(3):213-21. PMID:9501915
Page seeded by OCA on Mon Nov 5 16:44:14 2007