Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FFV

Crystal Structure Analysis of Syd

3FFV の概要
エントリーDOI10.2210/pdb3ffv/pdb
分子名称Protein syd (2 entities in total)
機能のキーワードmembrane, translocon, secyeg, syd, nanodisc, cell inner membrane, cell membrane, protein binding
由来する生物種Escherichia coli
細胞内の位置Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P0A8U0
タンパク質・核酸の鎖数2
化学式量合計41458.84
構造登録者
Maurus, R.,Brayer, G.D. (登録日: 2008-12-04, 公開日: 2009-01-27, 最終更新日: 2011-07-13)
主引用文献Dalal, K.,Nguyen, N.,Alami, M.,Tan, J.,Moraes, T.F.,Lee, W.C.,Maurus, R.,Sligar, S.S.,Brayer, G.D.,Duong, F.
Structure, Binding, and Activity of Syd, a SecY-interacting Protein
J.Biol.Chem., 284:7897-7902, 2009
Cited by
PubMed Abstract: The Syd protein has been implicated in the Sec-dependent transport of polypeptides across the bacterial inner membrane. Using Nanodiscs, we here provide direct evidence that Syd binds the SecY complex, and we demonstrate that interaction involves the two electropositive and cytosolic loops of the SecY subunit. We solve the crystal structure of Syd and together with cysteine cross-link analysis, we show that a conserved concave and electronegative groove constitutes the SecY-binding site. At the membrane, Syd decreases the activity of the translocon containing loosely associated SecY-SecE subunits, whereas in detergent solution Syd disrupts the SecYEG heterotrimeric associations. These results support the role of Syd in proofreading the SecY complex biogenesis and point to the electrostatic nature of the Sec channel interaction with its cytosolic partners.
PubMed: 19139097
DOI: 10.1074/jbc.M808305200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 3ffv
検証レポート(詳細版)ダウンロードをダウンロード

227111

件を2024-11-06に公開中

PDB statisticsPDBj update infoContact PDBjnumon