1V0H
ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID
Summary for 1V0H
| Entry DOI | 10.2210/pdb1v0h/pdb |
| Related | 1OAF 1OAG |
| Descriptor | ASCORBATE PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | oxidoreductase, heme peroxidase, peroxide scavenge, ascorbate peroxidase |
| Biological source | GLYCINE MAX (SOYBEAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 29154.52 |
| Authors | Sharp, K.H.,Raven, E.L.,Moody, P.C.E. (deposition date: 2004-03-29, release date: 2004-06-23, Last modification date: 2023-12-13) |
| Primary citation | Sharp, K.H.,Moody, P.C.E.,Brown, K.A.,Raven, E.L. Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex Biochemistry, 43:8644-, 2004 Cited by PubMed Abstract: 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. PubMed: 15236572DOI: 10.1021/BI049343Q PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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