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5CCO

Staphylococcus bacteriophage 80alpha dUTPase with dUMP.

5CCO の概要
エントリーDOI10.2210/pdb5cco/pdb
関連するPDBエントリー3ZEZ
分子名称DUTPase, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
機能のキーワードphage, pathogenicity island, sapi induction, gene transfer, moonlighting proteins, dut, dutp, g protein, p-loop, hydrolase
由来する生物種Staphylococcus phage 80alpha
タンパク質・核酸の鎖数1
化学式量合計19471.46
構造登録者
Maiques, E.,Quiles-Puchalt, N.,Donderis, J.,Ciges, J.R.,Alite, C.,Bowring, J.,Penades, J.R.,Marina, A. (登録日: 2015-07-02, 公開日: 2016-05-11, 最終更新日: 2024-01-10)
主引用文献Maiques, E.,Quiles-Puchalt, N.,Donderis, J.,Ciges-Tomas, J.R.,Alite, C.,Bowring, J.Z.,Humphrey, S.,Penades, J.R.,Marina, A.
Another look at the mechanism involving trimeric dUTPases in Staphylococcus aureus pathogenicity island induction involves novel players in the party.
Nucleic Acids Res., 44:5457-5469, 2016
Cited by
PubMed Abstract: We have recently proposed that the trimeric staphylococcal phage encoded dUTPases (Duts) are signaling molecules that act analogously to eukaryotic G-proteins, using dUTP as a second messenger. To perform this regulatory role, the Duts require their characteristic extra motif VI, present in all the staphylococcal phage coded trimeric Duts, as well as the strongly conserved Dut motif V. Recently, however, an alternative model involving Duts in the transfer of the staphylococcal islands (SaPIs) has been suggested, questioning the implication of motifs V and VI. Here, using state-of the-art techniques, we have revisited the proposed models. Our results confirm that the mechanism by which the Duts derepress the SaPI cycle depends on dUTP and involves both motifs V and VI, as we have previously proposed. Surprisingly, the conserved Dut motif IV is also implicated in SaPI derepression. However, and in agreement with the proposed alternative model, the dUTP inhibits rather than inducing the process, as we had initially proposed. In summary, our results clarify, validate and establish the mechanism by which the Duts perform regulatory functions.
PubMed: 27112567
DOI: 10.1093/nar/gkw317
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.33 Å)
構造検証レポート
Validation report summary of 5cco
検証レポート(詳細版)ダウンロードをダウンロード

248636

件を2026-02-04に公開中

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