2bur
From Proteopedia
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| - | [[Image:2bur.gif|left|200px]] | + | [[Image:2bur.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 IN COMPLEX WITH 4-HYDROXYBENZOATE''' | + | {{Structure |
| + | |PDB= 2bur |SIZE=350|CAPTION= <scene name='initialview01'>2bur</scene>, resolution 1.8Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Phb+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=PHB:P-HYDROXYBENZOIC ACID'>PHB</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF WILD-TYPE PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 IN COMPLEX WITH 4-HYDROXYBENZOATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BUR is a [ | + | 2BUR is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Acinetobacter_calcoaceticus Acinetobacter calcoaceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15487948 15487948] |
[[Category: Acinetobacter calcoaceticus]] | [[Category: Acinetobacter calcoaceticus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: non-heme iron]] | [[Category: non-heme iron]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:07:02 2008'' |
Revision as of 14:07, 20 March 2008
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| , resolution 1.8Å | |||||||
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| 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 IN COMPLEX WITH 4-HYDROXYBENZOATE
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
2BUR is a Protein complex structure of sequences from Acinetobacter calcoaceticus. 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 Mar 20 16:07:02 2008
Categories: Acinetobacter calcoaceticus | 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 | PHB | Aromatic degradation | Beta-sandwich | Dioxygenase | Mixed alpha/beta structure | Non-heme iron
