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1NMT

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

1NMT の概要
エントリーDOI10.2210/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
Weston, S.A.,Pauptit, R.A. (登録日: 1997-12-11, 公開日: 1999-01-13, 最終更新日: 2024-02-14)
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: 9501915
DOI: 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)
構造検証レポート
Validation report summary of 1nmt
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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