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)
Summary for 5SXY
| Entry DOI | 10.2210/pdb5sxy/pdb |
| NMR Information | BMRB: 30153 |
| Descriptor | Bifunctional coenzyme PQQ synthesis protein C/D (1 entity in total) |
| Functional Keywords | ripp rre peptide scaffolding, chaperone |
| Biological source | Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) |
| Total number of polymer chains | 1 |
| Total formula weight | 10421.94 |
| Authors | Evans, R.L.,Xia, Y.,Wilmot, C.M. (deposition date: 2016-08-10, release date: 2017-05-24, Last modification date: 2024-05-01) |
| Primary citation | Evans, R.L.,Latham, J.A.,Xia, Y.,Klinman, J.P.,Wilmot, C.M. Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone. Biochemistry, 56:2735-2746, 2017 Cited by PubMed Abstract: Biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is initiated when the precursor peptide, PqqA, is recognized and bound by the RiPP precursor peptide recognition element (RRE), PqqD, for presentation to the first enzyme in the pathway, PqqE. Unlike other RiPP-producing, postribosomal peptide synthesis (PRPS) pathways in which the RRE is a component domain of the first enzyme, PqqD is predominantly a separate scaffolding protein that forms a ternary complex with the precursor peptide and first tailoring enzyme. As PqqD is a stable, independent RRE, this makes the PQQ pathway an ideal PRPS model system for probing RRE interactions using nuclear magnetic resonance (NMR). Herein, we present both the solution NMR structure of Methylobacterium extorquens PqqD and results of H-N HSQC binding experiments that identify the PqqD residues involved in binding the precursor peptide, PqqA, and the enzyme, PqqE. The reported structural model for an independent RRE, along with the mapped binding surfaces, will inform future efforts both to understand and to manipulate PRPS pathways. PubMed: 28481092DOI: 10.1021/acs.biochem.7b00247 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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