6u01 | pdb_00006u01

Dihydrodipicolinate synthase (DHDPS) from C.jejuni, N84D mutant with pyruvate bound in the active site

spinqualitylabelsall models 6u01, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6u01 is a 6 chain structure with sequence from "campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, EDO, GOL, MG, PEG, PG4, PGE NonStd Res: KPI Gene: dapA_1, dapA, A6J93_04235, C9J79_06575, DDV78_09110, EBI45_07605, NCTC13362_01713 ("Campylobacter fetus subsp. jejuni" Smibert 1974) Activity: 4-hydroxy-tetrahydrodipicolinate synthase, with EC number 4.3.3.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0A2U0QMK8_CAMJU] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] Publication Abstract from PubMed 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 alpha-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. Asparagine-84, a regulatory allosteric site residue, helps maintain the quaternary structure of Campylobacter jejuni dihydrodipicolinate synthase.,Majdi Yazdi M, Saran S, Mrozowich T, Lehnert C, Patel TR, Sanders DAR, Palmer DRJ J Struct Biol. 2019 Oct 31:107409. doi: 10.1016/j.jsb.2019.107409. PMID:31678256 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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