1BOU
THREE-DIMENSIONAL STRUCTURE OF LIGAB
Summary for 1BOU
| Entry DOI | 10.2210/pdb1bou/pdb |
| Descriptor | 4,5-DIOXYGENASE ALPHA CHAIN, 4,5-DIOXYGENASE BETA CHAIN, FE (III) ION, ... (4 entities in total) |
| Functional Keywords | extradiol type dioxygenase, oxidoreductase, dioxygenase |
| Biological source | Sphingomonas paucimobilis More |
| Total number of polymer chains | 4 |
| Total formula weight | 97892.71 |
| Authors | Sugimoto, K.,Senda, T.,Fukuda, M.,Mitsui, Y. (deposition date: 1998-08-06, release date: 1999-05-04, Last modification date: 2024-02-07) |
| Primary citation | Sugimoto, K.,Senda, T.,Aoshima, H.,Masai, E.,Fukuda, M.,Mitsui, Y. Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure, 7:953-965, 1999 Cited by PubMed Abstract: Sphingomonas paucimobilis SYK-6 utilizes an extradiol-type catecholic dioxygenase, the LigAB enzyme (a protocatechuate 4,5-dioxygenase), to oxidize protocatechuate (or 3,4-dihydroxybenzoic acid, PCA). The enzyme belongs to the family of class III extradiol-type catecholic dioxygenases catalyzing the ring-opening reaction of protocatechuate and related compounds. The primary structure of LigAB suggests that the enzyme has no evolutionary relationship with the family of class II extradiol-type catecholic dioxygenases. Both the class II and class III enzymes utilize a non-heme ferrous center for adding dioxygen to the substrate. By elucidating the structure of LigAB, we aimed to provide a structural basis for discussing the function of class III enzymes. PubMed: 10467151DOI: 10.1016/S0969-2126(99)80122-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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