3GYR

Structure of Phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center.

Replaces:  2G23

Summary for 3GYR

• Entry DOI: 10.2210/pdb3gyr/pdb
• Related: 2G23
• Descriptor: Phenoxazinone synthase, COPPER (II) ION, CU-O-CU LINKAGE, ... (5 entities in total)
• Functional Keywords: metalloprotein, laccase, multicopper oxidase, hexamer, oxidoreductase, antibiotic biosynthesis, metal-binding
• Biological source: Streptomyces antibioticus
• Total number of polymer chains: 12
• Total formula weight: 810238.91

Authors

Smith, A.W.,Camara-Artigas, A.,Wang, M.,Francisco, W.A.,Allen, J.P. (deposition date: 2009-04-05, release date: 2009-04-28, Last modification date: 2023-09-06)

Primary citation

Smith, A.W.,Camara-Artigas, A.,Wang, M.,Allen, J.P.,Francisco, W.A.
Structure of Phenoxazinone Synthase from Streptomyces Antibioticus Reveals a New Type 2 Copper Center.
Biochemistry, 45:4378-, 2006

PubMed 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.

PubMed: 16584173

Experimental method

X-RAY DIFFRACTION (2.3 Å)