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Structure paper

TitleCharacterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 116, Page 17245-17250, Year 2019
Publish dateAug 7, 2018 (structure data deposition date)
AuthorsBothwell, I.R. / Cogan, D.P. / Kim, T. / Reinhardt, C.J. / van der Donk, W.A. / Nair, S.K.
External linksProc. Natl. Acad. Sci. USA / PubMed:31409709
MethodsX-ray diffraction
Resolution2.148 - 2.794 Å
Structure data

PDB-6ec7:
Glutamylation domain, TbtB, from thiomuracin biosynthesis
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

PDB-6ec8:
Glutamylation domain, TbtB, from thiomuracin biosynthesis bound to 5'-phosphodesmethylglutamycin
Method: X-RAY DIFFRACTION / Resolution: 2.148 Å

PDB-6m7y:
Dehydratase, NisB, bound to a non-eliminable substrate analog
Method: X-RAY DIFFRACTION / Resolution: 2.794 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-J4G:
3'-deoxy-3'-[(L-alpha-glutamyl)amino]adenosine 5'-(dihydrogen phosphate)

Source
  • thermobispora bispora (strain atcc 19993 / dsm 43833 / cbs 139.67 / jcm 10125 / nbrc 14880 / r51) (bacteria)
  • lactococcus lactis subsp. lactis (lactic acid bacteria)
  • lactococcus lactis (lactic acid bacteria)
KeywordsBIOSYNTHETIC PROTEIN / RiPP / thiopeptide / thiomuracin / tRNA-dependent / glutamylation / dehydratase / nisin

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