3NZI

Substrate induced remodeling of the active site regulates HtrA1 activity


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.75 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Substrate-induced remodeling of the active site regulates human HTRA1 activity.

Truebestein, L.Tennstaedt, A.Monig, T.Krojer, T.Canellas, F.Kaiser, M.Clausen, T.Ehrmann, M.

(2011) Nat Struct Mol Biol 18: 386-388

  • DOI: https://doi.org/10.1038/nsmb.2013
  • Primary Citation of Related Structures:  
    3NUM, 3NWU, 3NZI

  • PubMed Abstract: 

    Crystal structures of active and inactive conformations of the human serine protease HTRA1 reveal that substrate binding to the active site is sufficient to stimulate proteolytic activity. HTRA1 attaches to liposomes, digests misfolded proteins into defined fragments and undergoes substrate-mediated oligomer conversion. In contrast to those of other serine proteases, the PDZ domain of HTRA1 is dispensable for activation or lipid attachment, indicative of different underlying mechanistic features.


  • Organizational Affiliation

    Centre for Medical Biotechnology, Faculty of Biology, University Duisburg-Essen, Essen, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine protease HTRA1334Homo sapiensMutation(s): 0 
Gene Names: HTRA1HTRAPRSS11
EC: 3.4.21
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q92743 (Homo sapiens)
Explore Q92743 
Go to UniProtKB:  Q92743
PHAROS:  Q92743
GTEx:  ENSG00000166033 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ92743
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Citrate synthase7N/AMutation(s): 0 
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q9CZU6 (Mus musculus)
Explore Q9CZU6 
Go to UniProtKB:  Q9CZU6
IMPC:  MGI:88529
Entity Groups  
UniProt GroupQ9CZU6
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
B2V
Query on B2V
B
PEPTIDE-LIKEC4 H12 B N O2VAL
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.75 Å
  • R-Value Free: 0.249 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.202 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 105.965α = 90
b = 105.965β = 90
c = 118.336γ = 120
Software Package:
Software NamePurpose
PHASERphasing
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-02-23
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2018-04-18
    Changes: Data collection
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description
  • Version 1.4: 2023-11-22
    Changes: Data collection