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TitleAcyl Transfer Catalytic Activity in De Novo Designed Protein with N-Terminus of alpha-Helix As Oxyanion-Binding Site.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 143, Page 3330-3339, Year 2021
Publish dateMay 9, 2020 (structure data deposition date)
AuthorsNaudin, E.A. / McEwen, A.G. / Tan, S.K. / Poussin-Courmontagne, P. / Schmitt, J.L. / Birck, C. / DeGrado, W.F. / Torbeev, V.
External linksJ. Am. Chem. Soc. / PubMed:33635059
MethodsX-ray diffraction
Resolution1.45 - 2.33 Å
Structure data

PDB-6z0l:
Het-N2 - De novo designed three-helix heterodimer with Cysteine at the N2 position of the alpha-helix
Method: X-RAY DIFFRACTION / Resolution: 2.33 Å

PDB-6z0m:
Het-Ncap - De novo designed three-helix heterodimer with Cysteine at the Ncap position of the alpha-helix
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-7bey:
Het-N2-SO3- - De novo designed three-helix heterodimer with Cysteine S-sulfate at the N2 position of the alpha-helix
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-CD:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-ZN:
Unknown entry

Source
  • synthetic construct (others)
KeywordsDE NOVO PROTEIN / Acyl Transfer Activity / Domain Swapped Dimer / Oxyanion-Binding Site

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