2bum: Difference between revisions
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|PDB= 2bum |SIZE=350|CAPTION= <scene name='initialview01'>2bum</scene>, resolution 1.80Å | |PDB= 2bum |SIZE=350|CAPTION= <scene name='initialview01'>2bum</scene>, resolution 1.80Å | ||
|SITE= <scene name='pdbsite=AC1:Hyd+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Hyd+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HYD:HYDROXY+GROUP'>HYD</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=2bum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bum OCA], [http://www.ebi.ac.uk/pdbsum/2bum PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bum RCSB]</span> | |||
}} | }} | ||
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[[Category: Valley, M P.]] | [[Category: Valley, M P.]] | ||
[[Category: Vetting, M W.]] | [[Category: Vetting, M W.]] | ||
[[Category: aromatic degradation]] | [[Category: aromatic degradation]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
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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 Mon Mar 31 02:11:58 2008'' | ||
Revision as of 23:11, 30 March 2008
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| 2bum, resolution 1.80Å | |||||||||||||
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| Sites: | AC1 | ||||||||||||
| Ligands: | FE, HYD | ||||||||||||
| 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 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
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