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
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