1VYX

Solution structure of the KSHV K3 N-terminal domain


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 30 
  • Conformers Submitted: 28 
  • Selection Criteria: NO VIOLATIONS GREATER THAN 0.25A, NO ANGLE VIOLATIONS 

wwPDB Validation   3D Report Full Report


This is version 1.5 of the entry. See complete history


Literature

Solution Structure of the Kaposi'S Sarcoma-Associated Herpesvirus K3 N-Terminal Domain Reveals a Novel E2-Binding C4Hc3-Type Ring Domain

Dodd, R.B.Allen, M.D.Brown, S.E.Sanderson, C.M.Duncan, L.M.Lehner, P.J.Bycroft, M.Read, R.J.

(2004) J Biol Chem 279: 53840

  • DOI: https://doi.org/10.1074/jbc.M409662200
  • Primary Citation of Related Structures:  
    1VYX

  • PubMed Abstract: 

    RING domains are found in a large number of eukaryotic proteins. Most function as E3 ubiquitin-protein ligases, catalyzing the terminal step in the ubiquitination process. Structurally, these domains have been characterized as binding two zinc ions in a stable cross-brace motif. The tumorigenic human gamma-herpesvirus Kaposi's sarcoma-associated herpesvirus encodes a ubiquitin-protein ligase termed K3, which functions as an immune evasion molecule by ubiquitinating major histocompatibility complex class I. K3 possesses at its N terminus a domain related to cellular RING domains but with an altered zinc ligand arrangement. This domain was initially characterized as a plant homeodomain, a structure not previously known to function as an E3. Here, it is conclusively demonstrated that the K3 N-terminal domain is a variant member of the RING domain family and not a plant homeodomain. The domain is found to interact with the cellular ubiquitin-conjugating enzymes UbcH5A to -C and UbcH13, which dock to the equivalent surface as on classical cellular RING domains. Interaction with UbcH13 suggests a possible role for K3 in catalyzing Lys(63)-linked ubiquitination.


  • Organizational Affiliation

    Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2XY, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ORF K360Human gammaherpesvirus 8Mutation(s): 0 
UniProt
Find proteins for P90495 (Human herpesvirus 8 type P (isolate GK18))
Explore P90495 
Go to UniProtKB:  P90495
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP90495
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ZN
Query on ZN

Download Ideal Coordinates CCD File 
B [auth A],
C [auth A]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 30 
  • Conformers Submitted: 28 
  • Selection Criteria: NO VIOLATIONS GREATER THAN 0.25A, NO ANGLE VIOLATIONS 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-10-01
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-01-24
    Changes: Source and taxonomy
  • Version 1.4: 2018-05-02
    Changes: Data collection, Experimental preparation
  • Version 1.5: 2024-05-15
    Changes: Data collection, Database references, Derived calculations, Other