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'''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1''' | '''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1''' | ||
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[[Category: Valley, M P.]] | [[Category: Valley, M P.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
[[Category: | [[Category: Aromatic degradation]] | ||
[[Category: | [[Category: Beta-sandwich]] | ||
[[Category: | [[Category: Dioxygenase]] | ||
[[Category: | [[Category: Mixed alpha/beta structure]] | ||
[[Category: | [[Category: Non-heme iron]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:49:24 2008'' | |||
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Revision as of 17:49, 3 May 2008
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 Page seeded by OCA on Sat May 3 20:49:24 2008
