5WQN
Crystal structure of a carbonyl reductase from Pseudomonas aeruginosa PAO1 (condition II)
Summary for 5WQN
| Entry DOI | 10.2210/pdb5wqn/pdb |
| Related | 5WQM 5WQO 5WQP |
| Descriptor | Probable dehydrogenase (2 entities in total) |
| Functional Keywords | short chain dehydrogenase/reductase, 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 | 4 |
| Total formula weight | 97362.64 |
| Authors | Li, S.,Wang, Y.,Bartlam, M. (deposition date: 2016-11-27, release date: 2017-10-04, Last modification date: 2023-11-08) |
| Primary citation | Li, S.,Teng, X.,Su, L.,Mao, G.,Xu, Y.,Li, T.,Liu, R.,Zhang, Q.,Wang, Y.,Bartlam, M. Structure and characterization of a NAD(P)H-dependent carbonyl reductase from Pseudomonas aeruginosa PAO1. FEBS Lett., 591:1785-1797, 2017 Cited by PubMed Abstract: To investigate the function of the pa4079 gene from the opportunistic pathogen Pseudomonas aeruginosa PAO1, we determined its crystal structure and confirmed it to be a NAD(P)-dependent short-chain dehydrogenase/reductase. Structural similarity and activity for a broad range of substrates indicate that PA4079 functions as a carbonyl reductase. Comparison of apo- and holo-PA4079 shows that NADP stabilizes the active site specificity loop, and small molecule binding induces rotation of the Tyr183 side chain by approximately 90° out of the active site. Quantitative real-time PCR results show that pa4079 maintains high expression levels during antibiotic exposure. This work provides a starting point for understanding substrate recognition and selectivity by PA4079, as well as its possible reduction of antimicrobial drugs. PubMed: 28524228DOI: 10.1002/1873-3468.12683 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
