5LPC

Crystal structure of Vanadium-dependent Haloperoxidase from A. marina

Summary for 5LPC

• Entry DOI: 10.2210/pdb5lpc/pdb
• Related: 1UP8
• Descriptor: Vanadium-dependent bromoperoxidase, PHOSPHATE ION (2 entities in total)
• Functional Keywords: vanadium, enzyme catalysis, peroxidase, halogenation, oxidoreductase
• Biological source: Acaryochloris marina
• Total number of polymer chains: 1
• Total formula weight: 73164.59

Authors

Frank, A.,Groll, M. (deposition date: 2016-08-12, release date: 2016-08-24, Last modification date: 2024-11-13)

Primary citation

Frank, A.,Seel, C.J.,Groll, M.,Gulder, T.
Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.
Chembiochem, 17:2028-2032, 2016

PubMed Abstract: Vanadium-dependent haloperoxidases (VHPOs) are a class of halogenating enzymes found in fungi, lichen, algae, and bacteria. We report the cloning, purification, and characterization of a functional VHPO from the cyanobacterium Acaryochloris marina (AmVHPO), including its structure determination by X-ray crystallography. Compared to other VHPOs, the AmVHPO features a unique set of disulfide bonds that stabilize the dodecameric assembly of the protein. Easy access by high-yield recombinant expression, as well as resistance towards organic solvents and temperature, together with a distinct halogenation reactivity, make this enzyme a promising starting point for the development of biocatalytic transformations.

PubMed: 27542168
DOI: 10.1002/cbic.201600417

Experimental method

X-RAY DIFFRACTION (3.1 Å)