4QBJ

Crystal structure of N-myristoyl transferase from Aspergillus fumigatus complexed with a synthetic inhibitor

Summary for 4QBJ

• Entry DOI: 10.2210/pdb4qbj/pdb
• Descriptor: Glycylpeptide N-tetradecanoyltransferase, SULFATE ION, S-(2-OXO)PENTADECYLCOA, ... (5 entities in total)
• Functional Keywords: transferase, myristoyl-coa, myristate translocation, transferase-transferase inhibitor complex, transferase/transferase inhibitor
• Biological source: Aspergillus fumigatus
• Cellular location: Cytoplasm: Q9UVX3
• Total number of polymer chains: 1
• Total formula weight: 47490.08

Authors

Suzuki, M.,Shimada, T. (deposition date: 2014-05-08, release date: 2015-04-01, Last modification date: 2023-11-08)

Primary citation

Shimada, T.,Suzuki, M.,Katakura, S.
Structure of N-myristoyltransferase from Aspergillus fumigatus
Acta Crystallogr.,Sect.D, 71:754-761, 2015

PubMed Abstract: N-Myristoyltransferase (NMT) is an enzyme which translocates the 14-carbon saturated fatty acid myristate from myristoyl-CoA to the N-terminal glycine of substrate peptides. This myristoylation process is involved in protein modification in various eukaryotes, including animals and fungi. Furthermore, this enzyme has been shown to be essential to the growth of various species, such as Saccharomyces cerevisiae, which indicates that NMT is an attractive target for the development of a novel antifungal drug. In this study, the crystal structure of a ternary complex of NMT from Aspergillus fumigatus with S-(2-oxo)pentadecyl-CoA, a myristoyl-CoA analogue cofactor, and a synthetic inhibitor is reported at a resolution of 2.1 Å. The results advance the understanding of the specificity of NMT inhibitors and provide valuable information for structure-based drug design.

PubMed: 25849386
DOI: 10.1107/S1399004715000401

Experimental method

X-RAY DIFFRACTION (2.1 Å)