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  1. 原著論文

Neutron crystallography of photoactive yellow protein reveals unusual protonation state of Arg52 in the crystal

https://repo.qst.go.jp/records/48476
https://repo.qst.go.jp/records/48476
3f88d35a-27d8-4e35-83cb-f1e09681865e
Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-02-07
タイトル
タイトル Neutron crystallography of photoactive yellow protein reveals unusual protonation state of Arg52 in the crystal
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Yonezawa, Kento

× Yonezawa, Kento

WEKO 487360

Yonezawa, Kento

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Shimizu, Nobutaka

× Shimizu, Nobutaka

WEKO 487361

Shimizu, Nobutaka

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栗原, 和男

× 栗原, 和男

WEKO 487362

栗原, 和男

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Yamazaki, Yoichi

× Yamazaki, Yoichi

WEKO 487363

Yamazaki, Yoichi

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Kamikubo, Hironari

× Kamikubo, Hironari

WEKO 487364

Kamikubo, Hironari

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Kataoka, Mikio

× Kataoka, Mikio

WEKO 487365

Kataoka, Mikio

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栗原 和男

× 栗原 和男

WEKO 487366

en 栗原 和男

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抄録
内容記述タイプ Abstract
内容記述 Because of its high pKa, arginine (Arg) is believed to be protonated even in the hydrophobic environment of the protein interior. However, our neutron crystallographic structure of photoactive yellow protein, a light sensor, demonstrated that Arg52 adopts an electrically neutral form. We also showed that the hydrogen bond between the chromophore and Glu46 is a so-called low barrier hydrogen bond (LBHB). Because both the neutral Arg and LBHB are unusual in proteins, these observations remain controversial. To validate our findings, we carried out neutron crystallographic analysis of the E46Q mutant of PYP. The resultant structure revealed that the proportion of the cationic form is higher in E46Q than in WT, although the cationic and neutral forms of Arg52 coexist in E46Q. These observations were confirmed by the occupancy of the deuterium atom bound to the N η1 atom combined with an alternative conformation of the N(η2)D2 group comprising sp2 hybridisation. Based on these results, we propose that the formation of the LBHB decreases the proton affinity of Arg52, stabilizing the neutral form in the crystal.
書誌情報 Scientific Reports (Online Only URL:http://www.nature.com/srep/index.html)

巻 7, 号 1, p. 9361-1-9361-10, 発行日 2017-08
ISSN
収録物識別子タイプ ISSN
収録物識別子 2045-2322
PubMed番号
識別子タイプ PMID
関連識別子 28839266
DOI
識別子タイプ DOI
関連識別子 10.1038/s41598-017-09718-9
関連サイト
識別子タイプ URI
関連識別子 https://www.nature.com/articles/s41598-017-09718-9
関連名称 https://www.nature.com/articles/s41598-017-09718-9
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