6U01
Dihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant with pyruvate bound in the active site
Summary for 6U01
| Entry DOI | 10.2210/pdb6u01/pdb |
| Descriptor | 4-hydroxy-tetrahydrodipicolinate synthase, 1,2-ETHANEDIOL, TETRAETHYLENE GLYCOL, ... (9 entities in total) |
| Functional Keywords | dihydrodipicolinate synthase, tim barrel, tetrameric protein, lyase |
| Biological source | Campylobacter jejuni |
| Total number of polymer chains | 6 |
| Total formula weight | 207293.45 |
| Authors | Saran, S.,Majdi Yazdi, M.,Lehnert, L.,Palmer, D.R.J.,Sanders, D.A.R. (deposition date: 2019-08-13, release date: 2019-12-04, Last modification date: 2023-11-29) |
| Primary citation | Majdi Yazdi, M.,Saran, S.,Mrozowich, T.,Lehnert, C.,Patel, T.R.,Sanders, D.A.R.,Palmer, D.R.J. Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase. J.Struct.Biol., 209:107409-107409, 2020 Cited by PubMed Abstract: Dihydrodipicolinate synthase (DHDPS) from Campylobacter jejuni is a natively homotetrameric enzyme that catalyzes the first unique reaction of (S)-lysine biosynthesis and is feedback-regulated by lysine through binding to an allosteric site. High-resolution structures of the DHDPS-lysine complex have revealed significant insights into the binding events. One key asparagine residue, N84, makes hydrogen bonds with both the carboxyl and the α-amino group of the bound lysine. We generated two mutants, N84A and N84D, to study the effects of these changes on the allosteric site properties. However, under normal assay conditions, N84A displayed notably lower catalytic activity, and N84D showed no activity. Here we show that these mutations disrupt the quaternary structure of DHDPS in a concentration-dependent fashion, as demonstrated by size-exclusion chromatography, multi-angle light scattering, dynamic light scattering, small-angle X-ray scattering (SAXS) and high-resolution protein crystallography. PubMed: 31678256DOI: 10.1016/j.jsb.2019.107409 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
Download full validation report
