7P2P

Human Signal Peptidase Complex Paralog A (SPC-A)

7P2P の概要

• エントリーDOI: 10.2210/pdb7p2p/pdb
• 関連するPDBエントリー: 7P2Q
• EMDBエントリー: 13171 13172
• 分子名称: Signal peptidase complex catalytic subunit SEC11A, Signal peptidase complex subunit 3, Signal peptidase complex subunit 2, ... (5 entities in total)
• 機能のキーワード: endoplasmic reticulum, signal peptide, serine protease, membrane complex, membrane protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93339.05

構造登録者

Liaci, A.M.,Foerster, F. (登録日: 2021-07-06, 公開日: 2021-10-06, 最終更新日: 2024-11-13)

主引用文献

Liaci, A.M.,Steigenberger, B.,Telles de Souza, P.C.,Tamara, S.,Grollers-Mulderij, M.,Ogrissek, P.,Marrink, S.J.,Scheltema, R.A.,Forster, F.
Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage.
Mol.Cell, 81:3934-3948.e11, 2021

PubMed Abstract: The signal peptidase complex (SPC) is an essential membrane complex in the endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large variety of secretory pre-proteins with exquisite specificity. Although the determinants of this process have been established empirically, the molecular details of SP recognition and removal remain elusive. Here, we show that the human SPC exists in two functional paralogs with distinct proteolytic subunits. We determined the atomic structures of both paralogs using electron cryo-microscopy and structural proteomics. The active site is formed by a catalytic triad and abuts the ER membrane, where a transmembrane window collectively formed by all subunits locally thins the bilayer. Molecular dynamics simulations indicate that this unique architecture generates specificity for SPs based on the length of their hydrophobic segments.

PubMed: 34388369
DOI: 10.1016/j.molcel.2021.07.031

実験手法

ELECTRON MICROSCOPY (4.9 Å)