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PDBsum entry 1v0h
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Oxidoreductase
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PDB id
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1v0h
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the ascorbate peroxidase-Salicylhydroxamic acid complex.
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Authors
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K.H.Sharp,
P.C.Moody,
K.A.Brown,
E.L.Raven.
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Ref.
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Biochemistry, 2004,
43,
8644-8651.
[DOI no: ]
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PubMed id
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Abstract
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Ascorbate peroxidase is a bifunctional peroxidase that catalyzes the
H(2)O(2)-dependent oxidation of both ascorbate and various aromatic substrates.
The ascorbate binding site was recently identified as being close to the
gamma-heme edge [Sharp, K. H., Mewies, M., Moody, P. C. E., and Raven, E. L.
(2003)Nat. Struct. Biol. 10, 303-307]. In this work, the X-ray crystal structure
of recombinant soybean cytosolic ascorbate peroxidase (rsAPX) in complex with
salicylhydroxamic acid (SHA) has been determined to 1.46 A. The SHA molecule is
bound close to the delta-heme edge in a cavity that connects the distal side of
the heme to the surface of the protein. There are hydrogen bonds between the
phenolic hydroxide of the SHA and the main chain carbonyl of Pro132, between the
carbonyl oxygen of SHA and the side chain guanadinium group of Arg38, and
between the hydroxamic acid group and the indole nitrogen of Trp41. The
structure provides the first information about the location of the aromatic
binding site in ascorbate peroxidase and, together with our previous data
[Sharp, K. H., et al. (2003) Nat. Struct. Biol. 10, 303-307], completes the
structural description of the binding properties of ascorbate peroxidase. The
mechanistic implications of the results are discussed in terms of our current
understanding of how APX catalyzes oxidation of different types of substrates
bound at different locations.
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