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  1. 080 繊維学部
  2. 0801 学術論文

Solution Structure of IseA, an Inhibitor Protein of DL-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop

http://hdl.handle.net/10091/17748
688cdac3-98d2-42ae-9112-fda36bbffee4
名前 / ファイル ライセンス アクション
Solution_structure_IseA_inhibitor_protein.pdf Solution_structure_IseA_inhibitor_protein.pdf (3.4 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2014-07-23
タイトル
言語 en
タイトル Solution Structure of IseA, an Inhibitor Protein of DL-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop
言語
言語 eng
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
著者 Arai, Ryoichi

× Arai, Ryoichi

WEKO 40421

Arai, Ryoichi

Search repository
Fukui, Sadaharu

× Fukui, Sadaharu

WEKO 40422

Fukui, Sadaharu

Search repository
Kobayashi, Naoya

× Kobayashi, Naoya

WEKO 40423

Kobayashi, Naoya

Search repository
Sekiguchi, Junichi

× Sekiguchi, Junichi

WEKO 40424

Sekiguchi, Junichi

Search repository
信州大学研究者総覧へのリンク
氏名 Arai, Ryoichi
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.OVkUjFkV.html
出版者
出版者 AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
引用
内容記述タイプ Other
内容記述 JOURNAL OF BIOLOGICAL CHEMISTRY. 287(53):44736-44748 (2012)
書誌情報 JOURNAL OF BIOLOGICAL CHEMISTRY

巻 287, 号 53, p. 44736-44748, 発行日 2012-12-28
抄録
内容記述タイプ Abstract
内容記述 In Bacillus subtilis, LytE, LytF, CwlS, and CwlO are vegetative autolysins, DL-endopeptidases in the NlpC/P60 family, and play essential roles in cell growth and separation. IseA (YoeB) is a proteinaceous inhibitor against the DL-endopeptidases, peptidoglycan hydrolases. Overexpression of IseA caused significantly long chained cell morphology, because IseA inhibits the cell separation DL-endopeptidases post-translationally. Here, we report the first three-dimensional structure of IseA, determined by NMR spectroscopy. The structure includes a single domain consisting of three alpha-helices, one 3(10)-helix, and eight beta-strands, which is a novel fold like a "hacksaw." Noteworthy is a dynamic loop between beta 4 and the 3(10)-helix, which resembles a "blade." The electrostatic potential distribution shows that most of the surface is positively charged, but the region around the loop is negatively charged. In contrast, the LytF active-site cleft is expected to be positively charged. NMR chemical shift perturbation of IseA interacting with LytF indicated that potential interaction sites are located around the loop. Furthermore, the IseA mutants D100K/D102K and G99P/G101P at the loop showed dramatic loss of inhibition activity against LytF, compared with wild-type IseA, indicating that the beta 4-3(10) loop plays an important role in inhibition. Moreover, we built a complex structure model of IseA-LytF by docking simulation, suggesting that the beta 4-3(10) loop of IseA gets stuck deep in the cleft of LytF, and the active site is occluded. These results suggest a novel inhibition mechanism of the hacksaw-like structure, which is different from known inhibitor proteins, through interactions around the characteristic loop regions with the active-site cleft of enzymes.
資源タイプ(コンテンツの種類)
内容記述タイプ Other
内容記述 Article
ISSN
収録物識別子タイプ ISSN
収録物識別子 0021-9258
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA00251083
PubMed
関連識別子
識別子タイプ PMID
関連識別子 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=23091053
関連名称
関連名称 23091053
DOI
関連識別子
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.M112.414763
関連名称
関連名称 10.1074/jbc.M112.414763
権利
権利情報 This research was originally published in The Journal of Biological Chemistry. Arai, R. et al. Solution Structure of IseA, an Inhibitor Protein of DL-Endopeptidases from Bacillus subtilis, Reveals a Novel Fold with a Characteristic Inhibitory Loop. The Journal of Biological Chemistry. 2012; Vol:287 pp.44736-44748. Copyright© the American Society for Biochemistry and Molecular Biology.
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
WoS
表示名 Web of Science
URL http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000312938600068
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