1DMH

STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 WITH BOUND 4-METHYLCATECHOL

Summary for 1DMH

• Entry DOI: 10.2210/pdb1dmh/pdb
• Related: 1DLM 1DLQ 1DLT
• Descriptor: CATECHOL 1,2-DIOXYGENASE, FE (III) ION, 4-METHYLCATECHOL, ... (5 entities in total)
• Functional Keywords: dioxygenase, aromatic hydrocarbon degradation, alpha/beta fold, metalloenzyme, substrate, oxidoreductase
• Biological source: Acinetobacter sp.
• Total number of polymer chains: 2
• Total formula weight: 70401.98

Authors

Vetting, M.W.,Ohlendorf, D.H. (deposition date: 1999-12-14, release date: 2000-05-23, Last modification date: 2024-02-07)

Primary citation

Vetting, M.W.,Ohlendorf, D.H.
The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Structure Fold.Des., 8:429-440, 2000

PubMed Abstract: Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. Catechol 1,2-dioxygenases (1, 2-CTDs) have a rudimentary design structure - a homodimer with one catalytic non-heme ferric ion per monomer, that is (alphaFe(3+))(2). This is in contrast to the archetypical intradiol dioxygenase protocatechuate 3,4-dioxygenase (3,4-PCD), which forms more diverse oligomers, such as (alphabetaFe(3+))(2-12).

PubMed: 10801478
DOI: 10.1016/S0969-2126(00)00122-2

Experimental method

X-RAY DIFFRACTION (1.7 Å)