3JYQ
Quinate dehydrogenase from Corynebacterium glutamicum in complex with shikimate and NADH
Summary for 3JYQ
| Entry DOI | 10.2210/pdb3jyq/pdb |
| Related | 2nlo 3JYO 3JYP |
| Descriptor | Quinate/shikimate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID, ... (4 entities in total) |
| Functional Keywords | quinate dehyrogenase, ternary complex, shikimate, nadh, amino-acid biosynthesis, aromatic amino acid biosynthesis, nad, oxidoreductase |
| Biological source | Corynebacterium glutamicum (Brevibacterium flavum) |
| Total number of polymer chains | 1 |
| Total formula weight | 30562.16 |
| Authors | Hoeppner, A.,Schomburg, D.,Niefind, K. (deposition date: 2009-09-22, release date: 2010-10-27, Last modification date: 2023-09-06) |
| Primary citation | Hoppner, A.,Schomburg, D.,Niefind, K. Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination. Biol.Chem., 394:1505-1516, 2013 Cited by PubMed Abstract: Quinate dehydrogenase (QDH) catalyzes the reversible oxidation of quinate to 3-dehydroquinate by nicotineamide adenine dinucleotide (NADH) and is involved in the catabolic quinate metabolism required for the degradation of lignin. The enzyme is a member of the family of shikimate/quinate dehydrogenases (SDH/QDH) occurring in bacteria and plants. We characterized the dual-substrate quinate/shikimate dehydrogenase (QSDH) from Corynebacterium glutamicum (CglQSDH) kinetically and revealed a clear substrate preference of CglQSDH for quinate compared with shikimate both at the pH optimum and in a physiological pH range, which is a remarkable contrast to closely related SDH/QDH enzymes. With respect to the cosubstrate, CglQSDH is strictly NAD(H) dependent. These substrate and cosubstrate profiles correlate well with the details of three atomic resolution crystal structures of CglQSDH in different functional states we report here: with bound NAD+ (binary complex) and as ternary complexes with NADH plus either shikimate or quinate. The CglQSDH-NADH-quinate structure is the first complex structure of any member of the SDH/QDH family with quinate. Based on this novel structural information and systematic sequence and structure comparisons with closely related enzymes, we can explain the strict NAD(H) dependency of CglQSDH as well as its discrimination between shikimate and quinate. PubMed: 23929881DOI: 10.1515/hsz-2013-0170 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.16 Å) |
Structure validation
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