1NKT

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEX WITH ADPBS

1NKT の概要

• エントリーDOI: 10.2210/pdb1nkt/pdb
• 関連するPDBエントリー: 1NL3
• 分子名称: Preprotein translocase secA 1 subunit, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: preprotein translocation, atpase, transmembrane transport, helicase-like motor domain, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, protein transport
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P0A5Y8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 207830.76

構造登録者

Sharma, V.,Arockiasamy, A.,Ronning, D.R.,Savva, C.G.,Holzenburg, A.,Braunstein, M.,Jacobs Jr., W.R.,Sacchettini, J.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 2003-01-03, 公開日: 2003-03-04, 最終更新日: 2024-02-14)

主引用文献

Sharma, V.,Arockiasamy, A.,Ronning, D.R.,Savva, C.G.,Holzenburg, A.,Braunstein, M.,Jacobs Jr., W.R.,Sacchettini, J.C.
Crystal Structure of M. tuberculosis SecA, A Preprotein Translocating ATPase
Proc.Natl.Acad.Sci.USA, 100:2243-2248, 2003

PubMed Abstract: In bacteria, the majority of exported proteins are translocated by the Sec system, which recognizes the signal sequence of a preprotein and uses ATP and the proton motive force to mediate protein translocation across the cytoplasmic membrane. SecA is an essential protein component of this system, containing the molecular motor that facilitates translocation. Here we report the three-dimensional structure of the SecA protein of Mycobacterium tuberculosis. Each subunit of the homodimer contains a "motor" domain and a translocation domain. The structure predicts that SecA can interact with the SecYEG pore and function as a molecular ratchet that uses ATP hydrolysis for physical movement of the preprotein. Knowledge of this structure provides a framework for further elucidation of the translocation process.

PubMed: 12606717
DOI: 10.1073/pnas.0538077100

実験手法

X-RAY DIFFRACTION (2.601 Å)