5DCE
Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase regulated (Tryptophan)
Summary for 5DCE
| Entry DOI | 10.2210/pdb5dce/pdb |
| Related | 5DCC 5DCD |
| Descriptor | Phospho-2-dehydro-3-deoxyheptonate aldolase, MANGANESE (II) ION, TRYPTOPHAN, ... (4 entities in total) |
| Functional Keywords | allostery, aromatic amino acids, dah7ps, transferase |
| Biological source | Neisseria meningitidis serogroup B (strain MC58) |
| Total number of polymer chains | 4 |
| Total formula weight | 155885.18 |
| Authors | Heyes, L.C.,Parker, E.J. (deposition date: 2015-08-24, release date: 2016-08-24, Last modification date: 2024-03-06) |
| Primary citation | Cross, P.J.,Heyes, L.C.,Zhang, S.,Nazmi, A.R.,Parker, E.J. The Functional Unit of Neisseria meningitidis 3-Deoxy--Arabino-Heptulosonate 7-Phosphate Synthase Is Dimeric. Plos One, 11:e0145187-e0145187, 2016 Cited by PubMed Abstract: Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (NmeDAH7PS) adopts a homotetrameric structure consisting of an extensive and a less extensive interface. Perturbation of the less extensive interface through a single mutation of a salt bridge (Arg126-Glu27) formed at the tetramer interface of all chains resulted in a dimeric DAH7PS in solution, as determined by small angle X-ray scattering, analytical ultracentrifugation and analytical size-exclusion chromatography. The dimeric NmeDAH7PSR126S variant was shown to be catalytically active in the aldol-like condensation reaction between D-erythrose 4-phosphate and phosphoenolpyruvate, and allosterically inhibited by L-phenylalanine to the same extent as the wild-type enzyme. The dimeric NmeDAH7PSR126S variant exhibited a slight reduction in thermal stability by differential scanning calorimetry experiments and a slow loss of activity over time compared to the wild-type enzyme. Although NmeDAH7PSR126S crystallised as a tetramer, like the wild-type enzyme, structural asymmetry at the less extensive interface was observed consistent with its destabilisation. The tetrameric association enabled by this Arg126-Glu27 salt-bridge appears to contribute solely to the stability of the protein, ultimately revealing that the functional unit of NmeDAH7PS is dimeric. PubMed: 26828675DOI: 10.1371/journal.pone.0145187 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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