5lpc

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Crystal structure of Vanadium-dependent Haloperoxidase from A. marinaCrystal structure of Vanadium-dependent Haloperoxidase from A. marina

Structural highlights

5lpc is a 1 chain structure with sequence from Acaryochloris marina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B0C4R0_ACAM1

Publication Abstract from PubMed

Vanadium-dependent haloperoxidases (VHPOs) are an exquisite 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. The AmVHPO features a unique set of disulfide bonds, which 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.

Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.,Frank A, Seel CJ, Groll M, Gulder T Chembiochem. 2016 Aug 19. doi: 10.1002/cbic.201600417. PMID:27542168[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Frank A, Seel CJ, Groll M, Gulder T. Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential. Chembiochem. 2016 Aug 19. doi: 10.1002/cbic.201600417. PMID:27542168 doi:http://dx.doi.org/10.1002/cbic.201600417

5lpc, resolution 3.10Å

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