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5K9T

SecA-N68, a C-terminal truncation of the SecA ATPase from E. coli

5K9T の概要
エントリーDOI10.2210/pdb5k9t/pdb
分子名称Protein translocase subunit SecA, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
機能のキーワードpreprotein translocase, seca-n68, atpase, c-terminal truncation, n-terminus, peptide binding, protein transport
由来する生物種Escherichia coli (strain 55989 / EAEC)
細胞内の位置Cell inner membrane ; Peripheral membrane protein ; Cytoplasmic side : B7LFW8
タンパク質・核酸の鎖数1
化学式量合計64738.35
構造登録者
Shilton, B.H.,Vezina, G.C. (登録日: 2016-06-01, 公開日: 2017-06-07, 最終更新日: 2023-09-27)
主引用文献Yazdi, A.K.,Vezina, G.C.,Shilton, B.H.
An alternate mode of oligomerization for E. coli SecA.
Sci Rep, 7:11747-11747, 2017
Cited by
PubMed Abstract: SecA is the ATPase of preprotein translocase. SecA is a dimer in solution and changes in its oligomeric state may function in preprotein translocation. The SecA-N68 construct, in which the C-terminal helical domains of SecA are deleted, was used to investigate the mechanism of SecA oligomerization. SecA-N68 is in equilibrium between monomers, dimers, and tetramers. Subunit interactions in the SecA-N68 tetramer are mediated entirely by unstructured regions at its N- and C-termini: when the termini are deleted to yield SecA-N68∆NC, the construct is completely monomeric. This monomeric construct yielded crystals diffracting to 2.6 Å that were used to solve the structure of SecA-N68, including the "preprotein crosslinking domain" (PPXD) that was missing from previous E. coli SecA structures. The SecA-N68 structure was combined with small angle X-ray scattering (SAXS) data to construct a model of the SecA-N68 tetramer that is consistent with the essential roles of the extreme N- and C-termini in oligomerization. This mode of oligomerization, which depends on binding of the extreme N-terminus to the DEAD motor domains, NBD1 and NBD2, was used to model a novel parallel and flexible SecA solution dimer that agrees well with SAXS data.
PubMed: 28924213
DOI: 10.1038/s41598-017-11648-5
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 5k9t
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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