Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.3
Classification:OXIDOREDUCTASE
Release Date:2009-04-28
Deposition Date:2009-04-05
Revision Date:2011-07-13
Molecular Weight:810238.94
Macromolecule Type:Protein
Residue Count:7344
Atom Site Count:54864
DOI:10.2210/pdb3gyr/pdb
Abstract:
The multicopper oxidase phenoxazinone synthase (PHS) catalyzes the penultimate step in the biosynthesis of the antibiotic actinomycin D by Streptomyces antibioticus. PHS exists in two oligomeric forms: a dimeric form and a hexameric form, with older actinomycin-producing cultures containing predominately the hexameric form. The structure of hexameric PHS has been determined using X-ray diffraction to a resolution limit of 2.30 A and is found to contain several unexpected and distinctive features. The structure forms a hexameric ring that is centered on a pseudo 6-fold axis and has an outer diameter of 185 A with a large central cavity that has a diameter of 50 A. This hexameric structure is stabilized by a long loop connecting two domains; bound to this long loop is a fifth copper atom that is present as a type 2 copper. This copper atom is not present in any other multicopper oxidase, and its presence appears to stabilize the hexameric structure.
Resolution:2.3
Classification:OXIDOREDUCTASE
Release Date:2009-04-28
Deposition Date:2009-04-05
Revision Date:2011-07-13
Molecular Weight:810238.94
Macromolecule Type:Protein
Residue Count:7344
Atom Site Count:54864
DOI:10.2210/pdb3gyr/pdb
Abstract:
The multicopper oxidase phenoxazinone synthase (PHS) catalyzes the penultimate step in the biosynthesis of the antibiotic actinomycin D by Streptomyces antibioticus. PHS exists in two oligomeric forms: a dimeric form and a hexameric form, with older actinomycin-producing cultures containing predominately the hexameric form. The structure of hexameric PHS has been determined using X-ray diffraction to a resolution limit of 2.30 A and is found to contain several unexpected and distinctive features. The structure forms a hexameric ring that is centered on a pseudo 6-fold axis and has an outer diameter of 185 A with a large central cavity that has a diameter of 50 A. This hexameric structure is stabilized by a long loop connecting two domains; bound to this long loop is a fifth copper atom that is present as a type 2 copper. This copper atom is not present in any other multicopper oxidase, and its presence appears to stabilize the hexameric structure.
| Date made available | 2009 |
|---|---|
| Publisher | RCSB-PDB |