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TitleHigh-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation.
Journal, issue, pagesNat Commun, Vol. 11, Page 1132-1132, Year 2020
Publish dateSep 13, 2017 (structure data deposition date)
AuthorsDian, C. / Perez-Dorado, I. / Riviere, F. / Asensio, T. / Legrand, P. / Ritzefeld, M. / Shen, M. / Cota, E. / Meinnel, T. / Tate, E.W. / Giglione, C.
External linksNat Commun / PubMed:32111831
MethodsX-ray diffraction
Resolution1.87 - 2.8 Å
Structure data

PDB-6ehj:
Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and peptide bound
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6qrm:
HsNMT1 in complex with both MyrCoA and GNCFSKRRAA substrates
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-6sjz:
HsNMT1 in complex with both MyrCoA and Acetylated-GNCFSKPR substrates
Method: X-RAY DIFFRACTION / Resolution: 1.995 Å

PDB-6sk2:
HsNMT1 in complex with both MyrCoA and Acetylated-GKSFSKPR peptide reveals N-terminal Lysine Myristoylation
Method: X-RAY DIFFRACTION / Resolution: 1.90000651019 Å

PDB-6sk3:
C-terminal HsNMT1 deltaC3 truncation in complex with both MyrCoA and GNCFSKPR substrates
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-6sk8:
DeltaC3 C-terminal truncation of HsNMT1 in complex with MyrCoA and GDCFSKPR substrates
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-6skj:
DeltaC2 C-terminal truncation of HsNMT1 in complex with MyrCoA and GNCFSKPR substrates
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-MYA:
TETRADECANOYL-COA

ChemComp-GLY:
GLYCINE

ChemComp-SER:
SERINE

ChemComp-ASN:
ASPARAGINE

ChemComp-LYS:
LYSINE

ChemComp-PRO:
PROLINE

ChemComp-MYR:
MYRISTIC ACID

ChemComp-COA:
COENZYME A

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Myristoylation / complex / substrate peptide / Myristoyltransferase type1 / Acyltransferase / GNAT / GCN5-Related N-Acetyltransferases / NMT / E-MYRISTOYLATION

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