1LKD
CRYSTAL STRUCTURE OF 2,3-DIHYDROXYBIPHENYL 1,2-DIOXYGENASE (DHBD) COMPLEXED WITH 2',6'-DICL DIHYDROXYBIPHENYL (DHB)
Summary for 1LKD
| Entry DOI | 10.2210/pdb1lkd/pdb |
| Related | 1HAN 1KMY 1KND 1KNF 1LGT |
| Descriptor | BIPHENYL-2,3-DIOL 1,2-DIOXYGENASE, FE (II) ION, 2',6'-DICHLORO-BIPHENYL-2,6-DIOL, ... (5 entities in total) |
| Functional Keywords | extradiol dioxygenase, 2, 3-dihydroxybiphenyl, non-heme iron, anaerobic, pcb biodegradation, oxidoreductase |
| Biological source | Burkholderia xenovorans |
| Total number of polymer chains | 1 |
| Total formula weight | 33281.81 |
| Authors | Dai, S.,Bolin, J.T. (deposition date: 2002-04-24, release date: 2002-11-27, Last modification date: 2024-02-14) |
| Primary citation | Dai, S.,Vaillancourt, F.H.,Maaroufi, H.,Drouin, N.M.,Neau, D.B.,Snieckus, V.,Bolin, J.T.,Eltis, L.D. Identification and analysis of a bottleneck in PCB biodegradation Nat.Struct.Biol., 9:934-939, 2002 Cited by PubMed Abstract: The microbial degradation of polychlorinated biphenyls (PCBs) provides the potential to destroy these widespread, toxic and persistent environmental pollutants. For example, the four-step upper bph pathway transforms some of the more than 100 different PCBs found in commercial mixtures and is being engineered for more effective PCB degradation. In the critical third step of this pathway, 2,3-dihydroxybiphenyl (DHB) 1,2-dioxygenase (DHBD; EC 1.13.11.39) catalyzes aromatic ring cleavage. Here we demonstrate that ortho-chlorinated PCB metabolites strongly inhibit DHBD, promote its suicide inactivation and interfere with the degradation of other compounds. For example, k(cat)(app) for 2',6'-diCl DHB was reduced by a factor of approximately 7,000 relative to DHB, and it bound with sufficient affinity to competitively inhibit DHB cleavage at nanomolar concentrations. Crystal structures of two complexes of DHBD with ortho-chlorinated metabolites at 1.7 A resolution reveal an explanation for these phenomena, which have important implications for bioremediation strategies. PubMed: 12415290DOI: 10.1038/nsb866 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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