1B4U

PROTOCATECHUATE 4,5-DIOXYGENASE (LIGAB) IN COMPLEX WITH PROTOCATECHUATE (PCA)

Summary for 1B4U

• Entry DOI: 10.2210/pdb1b4u/pdb
• Descriptor: PROTOCATECHUATE 4,5-DIOXYGENASE, FE (III) ION, 3,4-DIHYDROXYBENZOIC ACID, ... (5 entities in total)
• Functional Keywords: extradiol type dioxygenase, protocatechuate, non-heme iron protein, dioxygenase
• Biological source: Sphingomonas paucimobilis; More
• Total number of polymer chains: 4
• Total formula weight: 98200.95

Authors

Sugimoto, K.,Senda, T.,Mitsui, Y. (deposition date: 1998-12-29, release date: 1999-08-27, 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 Fold.Des., 7:953-965, 1999

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: 10467151
DOI: 10.1016/S0969-2126(99)80122-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)