3ECJ
Structure of E323L mutant of Homoprotocatechuate 2,3-Dioxygenase from Brevibacterium fuscum at 1.65A resolution
Summary for 3ECJ
| Entry DOI | 10.2210/pdb3ecj/pdb |
| Related | 3ECK |
| Descriptor | PROTEIN (Homoprotocatechuate 2,3-dioxygenase), FE (II) ION, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, oxygenase, extradiol, feii, crystal packing, dioxygenase |
| Biological source | Brevibacterium fuscum |
| Total number of polymer chains | 4 |
| Total formula weight | 167915.29 |
| Authors | Kovaleva, E.G.,Lipscomb, J.D. (deposition date: 2008-08-31, release date: 2008-10-07, Last modification date: 2023-08-30) |
| Primary citation | Kovaleva, E.G.,Lipscomb, J.D. Intermediate in the O-O Bond Cleavage Reaction of an Extradiol Dioxygenase. Biochemistry, 47:11168-11170, 2008 Cited by PubMed Abstract: 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. PubMed: 18826259DOI: 10.1021/bi801459q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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