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2WSI

Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD

2WSI の概要
エントリーDOI10.2210/pdb2wsi/pdb
分子名称FAD SYNTHETASE, SULFATE ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total)
機能のキーワードtransferase, nucleotidyltransferase, nucleotide-binding
由来する生物種SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
細胞内の位置Cytoplasm: P38913
タンパク質・核酸の鎖数1
化学式量合計36462.64
構造登録者
Leulliot, N.,van Tilbeurgh, H. (登録日: 2009-09-07, 公開日: 2010-05-26, 最終更新日: 2024-05-08)
主引用文献Leulliot, N.,Blondeau, K.,Keller, J.,Ulryck, N.,Quevillon-Cheruel, S.,Van Tilbeurgh, H.
Crystal Structure of Yeast Fad Synthetase (Fad1) in Complex with Fad.
J.Mol.Biol., 398:641-, 2010
Cited by
PubMed Abstract: Flavin adenine dinucleotide (FAD) synthetase is an essential enzyme responsible for the synthesis of FAD by adenylation of riboflavin monophosphate (FMN). We have solved the 1.9 A resolution structure of Fad1, the yeast FAD synthetase, in complex with the FAD product in the active site. The structure of Fad1 shows it to be a member of the PP-ATPase superfamily. Important conformational differences in the two motifs involved in binding the phosphate moieties of FAD compared to the Candida glabrata FMNT ortholog suggests that this loop is dynamic and undergoes substantial conformational changes during its catalytic cycle.
PubMed: 20359485
DOI: 10.1016/J.JMB.2010.03.040
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 2wsi
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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