3OBQ

Crystal Structure of the Tsg101 UEV domain in complex with a human HRS PSAP peptide


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.207 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystallographic and Functional Analysis of the ESCRT-I /HIV-1 Gag PTAP Interaction.

Im, Y.J.Kuo, L.Ren, X.Burgos, P.V.Zhao, X.Z.Liu, F.Burke, T.R.Bonifacino, J.S.Freed, E.O.Hurley, J.H.

(2010) Structure 18: 1536-1547

  • DOI: https://doi.org/10.1016/j.str.2010.08.010
  • Primary Citation of Related Structures:  
    3OBQ, 3OBS, 3OBU, 3OBX

  • PubMed Abstract: 

    Budding of HIV-1 requires the binding of the PTAP late domain of the Gag p6 protein to the UEV domain of the TSG101 subunit of ESCRT-I. The normal function of this motif in cells is in receptor downregulation. Here, we report the 1.4-1.6 Å structures of the human TSG101 UEV domain alone and with wild-type and mutant HIV-1 PTAP and Hrs PSAP nonapeptides. The hydroxyl of the Thr or Ser residue in the P(S/T)AP motif hydrogen bonds with the main chain of Asn69. Mutation of the Asn to Pro, blocking the main-chain amide, abrogates PTAP motif binding in vitro and blocks budding of HIV-1 from cells. N69P and other PTAP binding-deficient alleles of TSG101 did not rescue HIV-1 budding. However, the mutant alleles did rescue downregulation of endogenous EGF receptor. This demonstrates that the PSAP motif is not rate determining in EGF receptor downregulation under normal conditions.


  • Organizational Affiliation

    Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0580, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tumor susceptibility gene 101 protein146Homo sapiensMutation(s): 0 
Gene Names: TSG101
UniProt & NIH Common Fund Data Resources
Find proteins for Q99816 (Homo sapiens)
Explore Q99816 
Go to UniProtKB:  Q99816
PHAROS:  Q99816
GTEx:  ENSG00000074319 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ99816
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Hepatocyte growth factor-regulated tyrosine kinase substrate9Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for O14964 (Homo sapiens)
Explore O14964 
Go to UniProtKB:  O14964
PHAROS:  O14964
GTEx:  ENSG00000185359 
Entity Groups  
UniProt GroupO14964
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.224 
  • R-Value Work: 0.207 
  • R-Value Observed: 0.207 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 33.654α = 90
b = 45.126β = 90
c = 87.734γ = 90
Software Package:
Software NamePurpose
MAR345dtbdata collection
MOLREPphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-12-01
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2015-05-27
    Changes: Source and taxonomy
  • Version 1.3: 2023-09-06
    Changes: Data collection, Database references, Refinement description