2NMT

MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE BOUND TO MYRISTOYL-COA AND PEPTIDE ANALOGS

2NMT の概要

• エントリーDOI: 10.2210/pdb2nmt/pdb
• 分子名称: MYRISTOYL-COA\:PROTEIN N-MYRISTOYLTRANSFERASE, S-(2-OXO)PENTADECYLCOA, [CYCLOHEXYLETHYL]-[[[[4-[2-METHYL-1-IMIDAZOLYL-BUTYL]PHENYL]ACETYL]-SERYL]-LYSINYL]-AMINE, ... (5 entities in total)
• 機能のキーワード: transferase acyltransferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P14743
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51707.82

構造登録者

Fuetterer, K.,Bhatnagar, R.S.,Waksman, G. (登録日: 1998-07-14, 公開日: 1999-01-06, 最終更新日: 2024-12-25)

主引用文献

Bhatnagar, R.S.,Futterer, K.,Farazi, T.A.,Korolev, S.,Murray, C.L.,Jackson-Machelski, E.,Gokel, G.W.,Gordon, J.I.,Waksman, G.
Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs.
Nat.Struct.Biol., 5:1091-1097, 1998

PubMed Abstract: N-myristoyltransferase (Nmt) attaches myristate to the N-terminal glycine of many important eukaryotic and viral proteins. It is a target for anti-fungal and anti-viral therapy. We have determined the structure, to 2.9 A resolution, of a ternary complex of Saccharomyces cerevisiae Nmt1p with bound myristoylCoA and peptide substrate analogs. The model reveals structural features that define the enzyme's substrate specificities and regulate the ordered binding and release of substrates and products. A novel catalytic mechanism is proposed involving deprotonation of the N-terminal ammonium of a peptide substrate by the enzyme's C-terminal backbone carboxylate.

PubMed: 9846880
DOI: 10.1038/4202

実験手法

X-RAY DIFFRACTION (2.9 Å)