2buv
From Proteopedia
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CRYSTAL STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 MUTANT R457S IN COMPLEX WITH PROTOCATECHUATE
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
2BUV is a [Protein complex] structure of sequences from [Acinetobacter calcoaceticus] with FE and DHB as [ligands]. Active as [[1]], with EC number [1.13.11.3]. 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
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