1NMT
N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A
1NMT の概要
| エントリーDOI | 10.2210/pdb1nmt/pdb |
| 分子名称 | N-MYRISTOYL TRANSFERASE, GLYCEROL (3 entities in total) |
| 機能のキーワード | myristylation, antifungal target, coa, transferase, acyltransferase |
| 由来する生物種 | Candida albicans |
| 細胞内の位置 | Cytoplasm: P30418 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 137922.39 |
| 構造登録者 | |
| 主引用文献 | Weston, S.A.,Camble, R.,Colls, J.,Rosenbrock, G.,Taylor, I.,Egerton, M.,Tucker, A.D.,Tunnicliffe, A.,Mistry, A.,Mancia, F.,de la Fortelle, E.,Irwin, J.,Bricogne, G.,Pauptit, R.A. Crystal structure of the anti-fungal target N-myristoyl transferase. Nat.Struct.Biol., 5:213-221, 1998 Cited by PubMed Abstract: 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. PubMed: 9501915DOI: 10.1038/nsb0398-213 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 Å) |
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