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TitleNuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.
Journal, issue, pagesBiochemistry, Vol. 56, Page 2735-2746, Year 2017
Publish dateAug 10, 2016 (structure data deposition date)
AuthorsEvans, R.L. / Latham, J.A. / Xia, Y. / Klinman, J.P. / Wilmot, C.M.
External linksBiochemistry / PubMed:28481092
MethodsNMR (solution)
Structure data

PDB-5sxy:
The solution NMR structure for the PqqD truncation of Methylobacterium extorquens PqqCD representing a functional and stand-alone ribosomally synthesized and post-translational modified (RiPP) recognition element (RRE)
Method: SOLUTION NMR

Source
  • methylobacterium extorquens (strain atcc 14718 / dsm 1338 / am1) (bacteria)
KeywordsCHAPERONE / RiPP RRE peptide scaffolding

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