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2buv
From Proteopedia
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|PDB= 2buv |SIZE=350|CAPTION= <scene name='initialview01'>2buv</scene>, resolution 1.8Å | |PDB= 2buv |SIZE=350|CAPTION= <scene name='initialview01'>2buv</scene>, resolution 1.8Å | ||
|SITE= <scene name='pdbsite=AC1:Dhb+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Dhb+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=DHB:3,4-DIHYDROXYBENZOIC+ACID'>DHB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2buv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2buv OCA], [http://www.ebi.ac.uk/pdbsum/2buv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2buv RCSB]</span> | ||
}} | }} | ||
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[[Category: Valley, M P.]] | [[Category: Valley, M P.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
| - | [[Category: DHB]] | ||
| - | [[Category: FE]] | ||
[[Category: aromatic degradation]] | [[Category: aromatic degradation]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
| Line 37: | Line 38: | ||
[[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 Mon Mar 31 02:12:04 2008'' |
Revision as of 23:12, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Protocatechuate 3,4-dioxygenase, with EC number 1.13.11.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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