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1bou

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:03:36 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:06:19 2007''

Revision as of 08:01, 30 October 2007

Image:1bou.gif

1bou, resolution 2.2Å

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THREE-DIMENSIONAL STRUCTURE OF LIGAB

Overview

BACKGROUND: 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., RESULTS: The ... [(full description)]

About this Structure

1BOU is a [Protein complex] structure of sequences from [Sphingomonas paucimobilis] with FE as [ligand]. Active as [Protocatechuate 4,5-dioxygenase], with EC number [1.13.11.8]. Structure known Active Sites: FEA and FEB. Full crystallographic information is available from [OCA].

Reference

Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions., Sugimoto K, Senda T, Aoshima H, Masai E, Fukuda M, Mitsui Y, Structure. 1999 Aug 15;7(8):953-65. PMID:10467151

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