4HYD

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

Summary for 4HYD

• Entry DOI: 10.2210/pdb4hyd/pdb
• Related: 4HYC 4HYG
• Descriptor: Putative uncharacterized protein (1 entity in total)
• Functional Keywords: protease, membrane protein
• Biological source: Methanoculleus marisnigri JR1
• Total number of polymer chains: 4
• Total formula weight: 127517.04

Authors

Li, X.,Dang, S.,Yan, C.,Wang, J.,Shi, Y. (deposition date: 2012-11-13, release date: 2012-12-19, Last modification date: 2024-03-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.8 Å)