1LVM

CATALYTICALLY ACTIVE TOBACCO ETCH VIRUS PROTEASE COMPLEXED WITH PRODUCT


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.171 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural basis for the substrate specificity of tobacco etch virus protease.

Phan, J.Zdanov, A.Evdokimov, A.G.Tropea, J.E.Peters III, H.K.Kapust, R.B.Li, M.Wlodawer, A.Waugh, D.S.

(2002) J Biol Chem 277: 50564-50572

  • DOI: https://doi.org/10.1074/jbc.M207224200
  • Primary Citation of Related Structures:  
    1LVB, 1LVM

  • PubMed Abstract: 

    Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant proteins. It is unclear, however, exactly how TEV protease recognizes its substrates with such high selectivity. The crystal structures of two TEV protease mutants, inactive C151A and autolysis-resistant S219D, have now been solved at 2.2- and 1.8-A resolution as complexes with a substrate and product peptide, respectively. The enzyme does not appear to have been perturbed by the mutations in either structure, and the modes of binding of the product and substrate are virtually identical. Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications.


  • Organizational Affiliation

    Macromolecular Crystallography Laboratory, Center for Cancer Research, NCI-Frederick, National Institutes of Health, Frederick, Maryland 21702-1201, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA)
A, B
229Tobacco etch virusMutation(s): 1 
UniProt
Find proteins for P04517 (Tobacco etch virus)
Explore P04517 
Go to UniProtKB:  P04517
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04517
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
OLIGOPEPTIDE SUBSTRATE FOR THE PROTEASE
C, D
10Tobacco etch virusMutation(s): 0 
UniProt
Find proteins for P04517 (Tobacco etch virus)
Explore P04517 
Go to UniProtKB:  P04517
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP04517
Sequence Annotations
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
CATALYTIC DOMAIN OF THE NUCLEAR INCLUSION PROTEIN A (NIA)7Tobacco etch virusMutation(s): 0 
UniProt
Find proteins for P04517 (Tobacco etch virus)
Explore P04517 
Go to UniProtKB:  P04517
Entity Groups  
UniProt GroupP04517
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.171 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 75.505α = 90
b = 75.505β = 90
c = 183.167γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
CNSrefinement

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-11-27
    Type: Initial release
  • Version 1.1: 2008-04-28
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-10-27
    Changes: Database references, Derived calculations