2BUT

Crystal Structure Of Protocatechuate 3,4-Dioxygenase from Acinetobacter Sp. ADP1 Mutant R457S - APO

Summary for 2BUT

• Entry DOI: 10.2210/pdb2but/pdb
• Related: 1EO2 1EO9 1EOA 1EOB 1EOC 2BUM 2BUQ 2BUR 2BUU 2BUV 2BUW 2BUX 2BUY 2BUZ 2BV0
• Descriptor: PROTOCATECHUATE 3,4-DIOXYGENASE ALPHA CHAIN, PROTOCATECHUATE 3,4-DIOXYGENASE BETA CHAIN, FE (III) ION, ... (5 entities in total)
• Functional Keywords: dioxygenase, aromatic degradation, non-heme iron, aromatic hydrocarbons catabolism, iron, oxidoreductase, metal-binding
• Biological source: ACINETOBACTER CALCOACETICUS; More
• Total number of polymer chains: 2
• Total formula weight: 51093.87

Authors

Vetting, M.W.,Valley, M.P.,D'Argenio, D.A.,Ornston, L.N.,Lipscomb, J.D.,Ohlendorf, D.H. (deposition date: 2005-06-17, release date: 2006-09-05, Last modification date: 2023-12-13)

Primary citation

Brown, C.K.,Vetting, M.W.,Earhart, C.A.,Ohlendorf, D.H.
Biophysical Analyses of Designed and Selected Mutants of Protocatechuate 3,4-Dioxygenase
Annu.Rev.Microbiol., 58:555-585, 2004

PubMed Abstract: The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

PubMed: 15487948
DOI: 10.1146/ANNUREV.MICRO.57.030502.090927

Experimental method

X-RAY DIFFRACTION (1.85 Å)