4HYG

Structure of a presenilin family intramembrane aspartate protease in C222 space group


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.32 Å
  • R-Value Free: 0.344 
  • R-Value Work: 0.298 
  • R-Value Observed: 0.301 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of a presenilin family intramembrane aspartate protease

Li, X.Dang, S.Yan, C.Gong, X.Wang, J.Shi, Y.

(2013) Nature 493: 56-61

  • DOI: https://doi.org/10.1038/nature11801
  • Primary Citation of Related Structures:  
    4HYC, 4HYD, 4HYG

  • 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.


  • Organizational Affiliation

    Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative uncharacterized protein
A, B, C, D
301Methanoculleus marisnigri JR1Mutation(s): 5 
Gene Names: Memar_1924
Membrane Entity: Yes 
UniProt
Find proteins for A3CWV0 (Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1))
Explore A3CWV0 
Go to UniProtKB:  A3CWV0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA3CWV0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.32 Å
  • R-Value Free: 0.344 
  • R-Value Work: 0.298 
  • R-Value Observed: 0.301 
  • Space Group: C 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 168.302α = 90
b = 201.892β = 90
c = 117.534γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-12-19
    Type: Initial release
  • Version 1.1: 2013-01-02
    Changes: Database references, Structure summary
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references