1nmt

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File:1nmt.gif


1nmt, resolution 2.45Å

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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, ... [(full description)]

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

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