6E2A
Crystal structure of NADH:quinone reductase PA1024 from Pseudomonas aeruginosa PAO1 in complex with NAD+
Summary for 6E2A
| Entry DOI | 10.2210/pdb6e2a/pdb |
| Descriptor | Nitronate monooxygenase, FLAVIN MONONUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | nadh:quinone reductase, quinone, oxidative stress, nad+ complex, flavoprotein, oxidoreductase |
| Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
| Total number of polymer chains | 1 |
| Total formula weight | 36993.73 |
| Authors | Reis, R.A.G.,Ball, J.,Agniswamy, J.,Weber, I.,Gadda, G. (deposition date: 2018-07-10, release date: 2019-02-06, Last modification date: 2023-10-11) |
| Primary citation | Ball, J.,Reis, R.A.G.,Agniswamy, J.,Weber, I.T.,Gadda, G. Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase. Protein Sci., 28:167-175, 2019 Cited by PubMed Abstract: The crystal structure of the NADH:quinone oxidoreductase PA1024 has been solved in complex with NAD to 2.2 Å resolution. The nicotinamide C4 is 3.6 Å from the FMN N5 atom, with a suitable orientation for facile hydride transfer. NAD binds in a folded conformation at the interface of the TIM-barrel domain and the extended domain of the enzyme. Comparison of the enzyme-NAD structure with that of the ligand-free enzyme revealed a different conformation of a short loop (75-86) that is part of the NAD -binding pocket. P78, P82, and P84 provide internal rigidity to the loop, whereas Q80 serves as an active site latch that secures the NAD within the binding pocket. An interrupted helix consisting of two α-helices connected by a small three-residue loop binds the pyrophosphate moiety of NAD . The adenine moiety of NAD appears to π-π stack with Y261. Steric constraints between the adenosine ribose of NAD , P78, and Q80, control the strict specificity of the enzyme for NADH. Charged residues do not play a role in the specificity of PA1024 for the NADH substrate. PubMed: 30246917DOI: 10.1002/pro.3514 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
