2buv: Difference between revisions
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==Overview== | ==Overview== | ||
The catechol dioxygenases allow a wide variety of bacteria to use aromatic | 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== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Protocatechuate 3,4-dioxygenase]] | [[Category: Protocatechuate 3,4-dioxygenase]] | ||
[[Category: Argenio, D | [[Category: Argenio, D A.D.]] | ||
[[Category: Lipscomb, J | [[Category: Lipscomb, J D.]] | ||
[[Category: Ohlendorf, D | [[Category: Ohlendorf, D H.]] | ||
[[Category: Ornston, L | [[Category: Ornston, L N.]] | ||
[[Category: Valley, M | [[Category: Valley, M P.]] | ||
[[Category: Vetting, M | [[Category: Vetting, M W.]] | ||
[[Category: DHB]] | [[Category: DHB]] | ||
[[Category: FE]] | [[Category: FE]] | ||
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[[Category: non-heme iron]] | [[Category: non-heme iron]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:51 2008'' | ||
Revision as of 14:41, 21 February 2008
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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 Protocatechuate 3,4-dioxygenase, with EC number 1.13.11.3 Known structural/functional Site: AC1. 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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