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-Structure paper
Title | High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation. |
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Journal, issue, pages | Nat Commun, Vol. 11, Page 1132-1132, Year 2020 |
Publish date | Sep 13, 2017 (structure data deposition date) |
Authors | Dian, C. / Perez-Dorado, I. / Riviere, F. / Asensio, T. / Legrand, P. / Ritzefeld, M. / Shen, M. / Cota, E. / Meinnel, T. / Tate, E.W. / Giglione, C. |
External links | Nat Commun / PubMed:32111831 |
Methods | X-ray diffraction |
Resolution | 1.87 - 2.8 Å |
Structure data | PDB-6ehj: PDB-6qrm: PDB-6sjz: PDB-6sk2: PDB-6sk3: PDB-6sk8: PDB-6skj: |
Chemicals | ChemComp-GOL: ChemComp-MYA: ChemComp-GLY: ChemComp-SER: ChemComp-ASN: ChemComp-LYS: ChemComp-PRO: ChemComp-MYR: ChemComp-COA: ChemComp-HOH: ChemComp-CL: ChemComp-MG: |
Source |
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Keywords | TRANSFERASE / Myristoylation / complex / substrate peptide / Myristoyltransferase type1 / Acyltransferase / GNAT / GCN5-Related N-Acetyltransferases / NMT / E-MYRISTOYLATION |