1V0H

ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID

1V0H の概要

• エントリーDOI: 10.2210/pdb1v0h/pdb
• 関連するPDBエントリー: 1OAF 1OAG
• 分子名称: ASCORBATE PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, heme peroxidase, peroxide scavenge, ascorbate peroxidase
• 由来する生物種: GLYCINE MAX (SOYBEAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29154.52

構造登録者

Sharp, K.H.,Raven, E.L.,Moody, P.C.E. (登録日: 2004-03-29, 公開日: 2004-06-23, 最終更新日: 2023-12-13)

主引用文献

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

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: 15236572
DOI: 10.1021/BI049343Q

実験手法

X-RAY DIFFRACTION (1.46 Å)