2bum

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PDB ID 2bum

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, resolution 1.80Å
Sites:
Ligands: and
Activity: Protocatechuate 3,4-dioxygenase, with EC number 1.13.11.3
Coordinates: save as pdb, mmCIF, xml



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.. 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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