2NMT

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

Summary for 2NMT

• Entry DOI: 10.2210/pdb2nmt/pdb
• Descriptor: 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)
• Functional Keywords: transferase acyltransferase, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P14743
• Total number of polymer chains: 1
• Total formula weight: 51707.82

Authors

Fuetterer, K.,Bhatnagar, R.S.,Waksman, G. (deposition date: 1998-07-14, release date: 1999-01-06, Last modification date: 2011-07-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.9 Å)