4HYD

Structure of a presenilin family intramembrane aspartate protease in C2221 space group

4HYD の概要

• エントリーDOI: 10.2210/pdb4hyd/pdb
• 関連するPDBエントリー: 4HYC 4HYG
• 分子名称: Putative uncharacterized protein (1 entity in total)
• 機能のキーワード: protease, membrane protein
• 由来する生物種: Methanoculleus marisnigri JR1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 127517.04

構造登録者

Li, X.,Dang, S.,Yan, C.,Wang, J.,Shi, Y. (登録日: 2012-11-13, 公開日: 2012-12-19, 最終更新日: 2024-03-20)

主引用文献

Li, X.,Dang, S.,Yan, C.,Gong, X.,Wang, J.,Shi, Y.
Structure of a presenilin family intramembrane aspartate protease
Nature, 493:56-61, 2013

PubMed Abstract: Presenilin and signal peptide peptidase (SPP) are intramembrane aspartyl proteases that regulate important biological functions in eukaryotes. Mechanistic understanding of presenilin and SPP has been hampered by lack of relevant structural information. Here we report the crystal structure of a presenilin/SPP homologue (PSH) from the archaeon Methanoculleus marisnigri JR1. The protease, comprising nine transmembrane segments (TMs), adopts a previously unreported protein fold. The amino-terminal domain, consisting of TM1-6, forms a horseshoe-shaped structure, surrounding TM7-9 of the carboxy-terminal domain. The two catalytic aspartate residues are located on the cytoplasmic side of TM6 and TM7, spatially close to each other and approximately 8 Å into the lipid membrane surface. Water molecules gain constant access to the catalytic aspartates through a large cavity between the amino- and carboxy-terminal domains. Structural analysis reveals insights into the presenilin/SPP family of intramembrane proteases.

PubMed: 23254940
DOI: 10.1038/nature11801

実験手法

X-RAY DIFFRACTION (3.8 Å)