1DIO

DIOL DEHYDRATASE-CYANOCOBALAMIN COMPLEX FROM KLEBSIELLA OXYTOCA

Summary for 1DIO

• Entry DOI: 10.2210/pdb1dio/pdb
• Descriptor: PROTEIN (DIOL DEHYDRATASE), POTASSIUM ION, S-1,2-PROPANEDIOL, ... (7 entities in total)
• Functional Keywords: coenzyme b12, propanediol, potassium ion, tim barrel, lyase
• Biological source: Klebsiella oxytoca; More
• Total number of polymer chains: 6
• Total formula weight: 210388.11

Authors

Shibata, N.,Masuda, J.,Tobimatsu, T.,Toraya, T.,Suto, K.,Morimoto, Y.,Yasuoka, N. (deposition date: 1999-01-27, release date: 2000-01-30, Last modification date: 2023-12-27)

Primary citation

Shibata, N.,Masuda, J.,Tobimatsu, T.,Toraya, T.,Suto, K.,Morimoto, Y.,Yasuoka, N.
A new mode of B12 binding and the direct participation of a potassium ion in enzyme catalysis: X-ray structure of diol dehydratase.
Structure Fold.Des., 7:997-1008, 1999

PubMed Abstract: Diol dehydratase is an enzyme that catalyzes the adenosylcobalamin (coenzyme B12) dependent conversion of 1,2-diols to the corresponding aldehydes. The reaction initiated by homolytic cleavage of the cobalt-carbon bond of the coenzyme proceeds by a radical mechanism. The enzyme is an alpha2beta2gamma2 heterooligomer and has an absolute requirement for a potassium ion for catalytic activity. The crystal structure analysis of a diol dehydratase-cyanocobalamin complex was carried out in order to help understand the mechanism of action of this enzyme.

PubMed: 10467140
DOI: 10.1016/S0969-2126(99)80126-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)