1TM6

NMR Structure of the Free Zinc Binding C-terminal Domain of SecA

1TM6 の概要

• エントリーDOI: 10.2210/pdb1tm6/pdb
• NMR情報: BMRB: 6289
• 分子名称: Preprotein translocase secA subunit, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, beta hairpin, seca, protein transport
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side: P10408
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2504.22

構造登録者

Matousek, W.M.,Alexandrescu, A.T. (登録日: 2004-06-10, 公開日: 2004-10-12, 最終更新日: 2024-05-22)

主引用文献

Matousek, W.M.,Alexandrescu, A.T.
NMR structure of the C-terminal domain of SecA in the free state
Biochim.Biophys.Acta, 1702:163-171, 2004

PubMed Abstract: SecA is an integral component of the prokaryotic Sec preprotein secretory translocase system. We report here the solution NMR structure of a fragment corresponding to the C-terminal domain of Escherichia coli SecA. In the presence of Zn2+, the fragment adopts a shortened version of the classic betabetaalpha zinc finger fold. The isolated C-terminal domain shows substantial differences from the X-ray structure of a homologous SecA domain bound to the chaperone-like cofactor SecB. The differences between the structures of the free and bound forms suggest that binding to SecB causes a perturbation of the C-terminal domain's intrinsically favored betabetaalpha fold.

PubMed: 15488768
DOI: 10.1016/j.bbapap.2004.08.012

実験手法

SOLUTION NMR