Structural highlights
3eck is a 4 chain structure with sequence from Brevibacterium fuscum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.6Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q45135_9MICO
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The reactive oxy intermediate of the catalytic cycle of extradiol aromatic ring-cleaving dioxygenases is formed by binding the catecholic substrate and O2 in adjacent ligand positions of the active site metal [usually Fe(II)]. This intermediate and the following Fe(II)-alkylperoxo intermediate resulting from oxygen attack on the substrate have been previously characterized in a crystal of homoprotocatechuate 2,3-dioxygenase (HPCD). Here a subsequent intermediate in which the O-O bond is broken to yield a gem diol species is structurally characterized. This new intermediate is stabilized in the crystal by using the alternative substrate, 4-sulfonylcatechol, and the Glu323Leu variant of HPCD, which alters the crystal packing.
Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase.,Kovaleva EG, Lipscomb JD Biochemistry. 2008 Oct 28;47(43):11168-70. Epub 2008 Oct 1. PMID:18826259[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kovaleva EG, Lipscomb JD. Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Biochemistry. 2008 Oct 28;47(43):11168-70. Epub 2008 Oct 1. PMID:18826259 doi:10.1021/bi801459q
