ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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言語種別 | 英語 |
発行・発表の年月 | 2016/01 |
形態種別 | 研究論文 |
査読 | 査読あり |
標題 | Anabaena sp. DyP-type peroxidase is a tetramer consisting of two asymmetric dimers. |
執筆形態 | その他 |
掲載誌名 | Proteins |
出版社・発行元 | WILEY |
巻・号・頁 | 84(1),pp.31-42 |
著者・共著者 | Yoshida T,Ogola HJ,Amano Y,Hisabori T,Ashida H,Sawa Y,Tsuge H,Sugano Y |
概要 | DyP-type peroxidases are a newly discovered family of heme peroxidases distributed from prokaryotes to eukaryotes. Recently, using a structure-based sequence alignment, we proposed the new classes, P, I and V, as substitutes for classes A, B, C, and D [Arch Biochem Biophys 2015;574:49-55]. Although many class V enzymes from eukaryotes have been characterized, only two from prokaryotes have been reported. Here, we show the crystal structure of one of these two enzymes, Anabaena sp. DyP-type peroxidase (AnaPX). AnaPX is tetramer formed from Cys224-Cys224 disulfide-linked dimers. The tetramer of wild-type AnaPX was stable at all salt concentrations tested. In contrast, the C224A mutant showed salt concentration-dependent oligomeric states: in 600 mM NaCl, it maintained a tetrameric structure, whereas in the absence of salt, it dissociated into monomers, leading to a reduction in thermostability. Although the tetramer exhibits non-crystallographic, 2-fold symmetry in the asymmetric unit, two subunits forming the Cys224-Cys224 disulfide-linked dimer are related by 165 degrees rotation. This asymmetry creates an opening to cavities facing the inside of the tetramer, providing a pathway for hydrogen peroxide access. Finally, a phylogenetic analysis using structure-based sequence alignments showed that class V enzymes from prokaryotes, including AnaPX, are phylogenetically closely related to class V enzymes from eukaryotes. Proteins 2016; 84:31-42. (c) 2015 Wiley Periodicals, Inc. |
DOI | 10.1002/prot.24952 |
ISSN | 0887-3585/1097-0134 |
PMID | 26492416 |
Put Code(ORCID) | 26473845 |
PermalinkURL | http://europepmc.org/abstract/med/26492416 |