2bum
From Proteopedia
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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: FE]] | [[Category: FE]] | ||
[[Category: HYD]] | [[Category: HYD]] | ||
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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 16:41:46 2008'' |
Revision as of 14:41, 21 February 2008
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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 Thu Feb 21 16:41:46 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
