1VNC

CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS

Summary for 1VNC

• Entry DOI: 10.2210/pdb1vnc/pdb
• Descriptor: VANADIUM-CONTAINING CHLOROPEROXIDASE, VANADATE ION, AZIDE ION, ... (4 entities in total)
• Functional Keywords: vanadium-containing haloperoxidase, oxidoreductase
• Biological source: Curvularia inaequalis
• Cellular location: Secreted: P49053
• Total number of polymer chains: 1
• Total formula weight: 67784.40

Authors

Messerschmidt, A.,Wever, R. (deposition date: 1995-09-01, release date: 1996-11-08, Last modification date: 2024-02-14)

Primary citation

Messerschmidt, A.,Wever, R.
X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
Proc.Natl.Acad.Sci.USA, 93:392-396, 1996

PubMed Abstract: The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis belongs to a class of vanadium enzymes that oxidize halides in the presence of hydrogen peroxide to the corresponding hypohalous acids. The 2.1 A crystal structure (R = 20%) of an azide chloroperoxidase complex reveals the geometry of the catalytic vanadium center. Azide coordinates directly to the metal center, resulting in a structure with azide, three nonprotein oxygens, and a histidine as ligands. In the native state vanadium will be bound as hydrogen vanadate(V) in a trigonal bipyramidal coordination with the metal coordinated to three oxygens in the equatorial plane, to the OH group at one apical position, and to the epsilon 2 nitrogen of a histidine at the other apical position. The protein fold is mainly alpha-helical with two four-helix bundles as main structural motifs and an overall structure different from other structures. The helices pack together to a compact molecule, which explains the high stability of the protein. An amino acid sequence comparison with vanadium-containing bromoperoxidase from the seaweed Ascophyllum nodosum shows high similarities in the regions of the metal binding site, with all hydrogen vanadate(V) interacting residues conserved except for lysine-353, which is an asparagine.

PubMed: 8552646
DOI: 10.1073/pnas.93.1.392

Experimental method

X-RAY DIFFRACTION (2.1 Å)