› 2wsa

X-ray diffraction
1.6Å resolution

Crystal Structure of Leishmania major N-myristoyltransferase (NMT) with bound myristoyl-CoA and a pyrazole sulphonamide ligand (DDD85646)

Released:
DOI: 10.2210/pdb2wsa/pdb
PDB entry 2wsa coloured by chain, front view.
PDB entry 2wsa coloured by chain, side view.
PDB entry 2wsa coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
N-myristoyltransferase inhibitors as new leads to treat sleeping sickness.
Frearson JA, Brand S, McElroy SP, Cleghorn LA, Smid O, Stojanovski L, Price HP, Guther ML, Torrie LS, Robinson DA, Hallyburton I, Mpamhanga CP, Brannigan JA, Wilkinson AJ, Hodgkinson M, Hui R, Qiu W, Raimi OG, van Aalten DM, Brenk R, Gilbert IH, Read KD, Fairlamb AH, Ferguson MA, Smith DF, Wyatt PG
Nature 464 728-32 (2010)
PMID: 20360736

Function and Biology Details

Reaction catalysed: 
Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 438 amino acids
Theoretical weight: 50.53 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4Q5S8 (Residues: 3-421; Coverage: 100%)
Gene names: LMJF_32_0080, NMT
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand MYA 1 x MYA
1 bound ligand:
Ligand 646 1 x 646
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 47.51Å b: 90.317Å c: 52.972Å
α: 90° β: 112.27° γ: 90°
R-values:
R R work R free
0.177 0.176 0.213
Expression system: Escherichia coli

Quick links

Citations

51 review citations

ARF family G proteins and their regulators: roles in membrane transport, development and disease.
Donaldson et al. (2011)
50 more

19 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
18 more