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3ILD

Structure of ORF157-K57A from Acidianus filamentous virus 1

3ILD の概要
エントリーDOI10.2210/pdb3ild/pdb
関連するPDBエントリー3II2 3II3 3ILE
分子名称Putative uncharacterized protein, MAGNESIUM ION (2 entities in total)
機能のキーワードvirus, archaea, nuclease, dna binding protein
由来する生物種Acidianus filamentous virus 1 (AFV-1)
タンパク質・核酸の鎖数1
化学式量合計18827.81
構造登録者
Goulet, A.,Lichiere, J.,Prangishvili, D.,van Tilbeurgh, H.,Cambillau, C.,Campanacci, V. (登録日: 2009-08-07, 公開日: 2010-03-23, 最終更新日: 2023-11-01)
主引用文献Goulet, A.,Pina, M.,Redder, P.,Prangishvili, D.,Vera, L.,Lichiere, J.,Leulliot, N.,van Tilbeurgh, H.,Ortiz-Lombardia, M.,Campanacci, V.,Cambillau, C.
ORF157 from the archaeal virus Acidianus filamentous virus 1 defines a new class of nuclease
J.Virol., 84:5025-5031, 2010
Cited by
PubMed Abstract: Acidianus filamentous virus 1 (AFV1) (Lipothrixviridae) is an enveloped filamentous virus that was characterized from a crenarchaeal host. It infects Acidianus species that thrive in the acidic hot springs (>85 degrees C and pH <3) of Yellowstone National Park, WY. The AFV1 20.8-kb, linear, double-stranded DNA genome encodes 40 putative open reading frames whose sequences generally show little similarity to other genes in the sequence databases. Because three-dimensional structures are more conserved than sequences and hence are more effective at revealing function, we set out to determine protein structures from putative AFV1 open reading frames (ORF). The crystal structure of ORF157 reveals an alpha+beta protein with a novel fold that remotely resembles the nucleotidyltransferase topology. In vitro, AFV1-157 displays a nuclease activity on linear double-stranded DNA. Alanine substitution mutations demonstrated that E86 is essential to catalysis. AFV1-157 represents a novel class of nuclease, but its exact role in vivo remains to be determined.
PubMed: 20200253
DOI: 10.1128/JVI.01664-09
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.1 Å)
構造検証レポート
Validation report summary of 3ild
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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