2bum
From Proteopedia
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CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1
Overview
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.
About this Structure
2BUM is a Protein complex structure of sequences from Acinetobacter calcoaceticus and Acinetobacter sp. with and as ligands. Active as Protocatechuate 3,4-dioxygenase, with EC number 1.13.11.3 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1., Brown CK, Vetting MW, Earhart CA, Ohlendorf DH, Annu Rev Microbiol. 2004;58:555-85. PMID:15487948
Page seeded by OCA on Sun Feb 3 10:27:57 2008
Categories: Acinetobacter calcoaceticus | Acinetobacter sp. | Protein complex | Protocatechuate 3,4-dioxygenase | Argenio, D.A.D. | Lipscomb, J.D. | Ohlendorf, D.H. | Ornston, L.N. | Valley, M.P. | Vetting, M.W. | FE | HYD | Aromatic degradation | Beta-sandwich | Dioxygenase | Mixed alpha/beta structure | Non-heme iron
