ログイン
Language:

WEKO3

  • トップ
  • ランキング
To
lat lon distance
To

Field does not validate



インデックスリンク

インデックスツリー

メールアドレスを入力してください。

WEKO

One fine body…

WEKO

One fine body…

アイテム

  1. 原著論文

Effects of targeting signal mutations in a mitochondrial presequence on the spatial distribution of the conformational ensemble in the binding site of Tom20.

https://repo.qst.go.jp/records/2000386
https://repo.qst.go.jp/records/2000386
a0ca336e-9deb-4407-a21b-b52045564539
アイテムタイプ 学術雑誌論文 / Journal Article(1)
公開日 2024-01-25
タイトル
タイトル Effects of targeting signal mutations in a mitochondrial presequence on the spatial distribution of the conformational ensemble in the binding site of Tom20.
言語 en
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
著者 Xiling Han

× Xiling Han

Xiling Han

Search repository
Maita Nobuo

× Maita Nobuo

Maita Nobuo

Search repository
Atsushi Shimada

× Atsushi Shimada

Atsushi Shimada

Search repository
Daisuke Kohda

× Daisuke Kohda

Daisuke Kohda

Search repository
抄録
内容記述タイプ Abstract
内容記述 The 20-kDa TOM (translocase of outer mitochondrial membrane) subunit, Tom20, is the first receptor of the protein import pathway into mitochondria. Tom20 recognizes the mitochondrial targeting signal embedded in the presequences attached to mature mitochondrial proteins, as an N-terminal extension. Consequently, ~1,000 different mitochondrial proteins are sorted into the mitochondrial matrix, and distinguished from non-mitochondrial proteins. We previously reported the MPRIDE (multiple partial recognitions in dynamic equilibrium) mechanism to explain the structural basis of the promiscuous recognition of presequences by Tom20. A subset of the targeting signal features is recognized in each pose of the presequence in the binding state, and all of the features are collectively recognized in the dynamic equilibrium between the poses. Here, we changed the volumes of the hydrophobic side chains in the targeting signal, while maintaining the binding affinity. We tethered the mutated presequences to the binding site of Tom20 and placed them in the crystal contact-free space (CCFS) created in the crystal lattice. The spatial distributions of the mutated presequences were visualized as smeared electron densities in the low-pass filtered difference maps obtained by X-ray crystallography. The mutated presequence ensembles shifted their positions in the binding state to accommodate the larger side chains, thus providing positive evidence supporting the use of the MPRIDE mechanism in the promiscuous recognition by Tom20.
書誌情報 Protein Science

巻 31, 号 10, p. e4433, 発行日 2022-10
出版者
出版者 John Wiley & Sons
ISSN
収録物識別子タイプ ISSN
収録物識別子 0961-8368
PubMed番号
識別子タイプ PMID
関連識別子 36173160
DOI
識別子タイプ DOI
関連識別子 10.1002/pro.4433
戻る
0
views
See details
Views

Versions

Ver.1 2025-08-15 02:18:05.657669
Show All versions

Share

Share
tweet

Cite as

Other

print

エクスポート

OAI-PMH
  • OAI-PMH JPCOAR 2.0
  • OAI-PMH JPCOAR 1.0
  • OAI-PMH DublinCore
  • OAI-PMH DDI
Other Formats
  • JSON
  • BIBTEX
  • ZIP

コミュニティ

確認

確認

確認


Powered by WEKO3


Powered by WEKO3