1VYX

Solution structure of the KSHV K3 N-terminal domain

Summary for 1VYX

• Entry DOI: 10.2210/pdb1vyx/pdb
• Related: 1CHC
• Descriptor: ORF K3, ZINC ION (2 entities in total)
• Functional Keywords: zinc-binding protein, ring domain, cross-brace motif
• Biological source: HUMAN HERPESVIRUS 8 (KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS)
• Cellular location: Host cell membrane ; Multi-pass membrane protein : P90495
• Total number of polymer chains: 1
• Total formula weight: 6963.51

Authors

Dodd, R.B.,Allen, M.D.,Brown, S.E.,Sanderson, C.M.,Duncan, L.M.,lehner, P.J.,Bycroft, M.,Read, R.J. (deposition date: 2004-05-07, release date: 2004-10-01, Last modification date: 2024-05-15)

Primary citation

Dodd, R.B.,Allen, M.D.,Brown, S.E.,Sanderson, C.M.,Duncan, L.M.,Lehner, P.J.,Bycroft, M.,Read, R.J.
Solution Structure of the Kaposi'S Sarcoma-Associated Herpesvirus K3 N-Terminal Domain Reveals a Novel E2-Binding C4Hc3-Type Ring Domain
J.Biol.Chem., 279:53840-, 2004

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.

PubMed: 15465811
DOI: 10.1074/JBC.M409662200

Experimental method

SOLUTION NMR