3SQV

Crystal Structure of E. coli O157:H7 E3 ubiquitin ligase, NleL, with a human E2, UbcH7

Summary for 3SQV

• Entry DOI: 10.2210/pdb3sqv/pdb
• Descriptor: secreted effector protein, Ubiquitin-conjugating enzyme E2 L3, SULFATE ION, ... (5 entities in total)
• Functional Keywords: effector protein, pentapeptide, hect domain, hect e3 ubiquitin ligase, e2 ubiquitin conjugating enzyme, protein-protein complex, ubiquitin transfer, ubiquitin, ubiquitination, ligase-signaling protein complex, ligase/signaling protein
• Biological source: Escherichia coli; More
• Cellular location: Nucleus: P68036
• Total number of polymer chains: 4
• Total formula weight: 176608.76

Authors

Lin, D.Y.,Chen, J. (deposition date: 2011-07-06, release date: 2012-01-25, Last modification date: 2024-11-20)

Primary citation

Lin, D.Y.,Diao, J.,Chen, J.
Crystal structures of two bacterial HECT-like E3 ligases in complex with a human E2 reveal atomic details of pathogen-host interactions.
Proc.Natl.Acad.Sci.USA, 109:1925-1930, 2012

PubMed Abstract: In eukaryotes, ubiquitination is an important posttranslational process achieved through a cascade of ubiquitin-activating (E1), conjugating (E2), and ligase (E3) enzymes. Many pathogenic bacteria deliver virulence factors into the host cell that function as E3 ligases. How these bacterial "Trojan horses" integrate into the eukaryotic ubiquitin system has remained a mystery. Here we report crystal structures of two bacterial E3s, Salmonella SopA and Escherichia coli NleL, both in complex with human E2 UbcH7. These structures represent two distinct conformational states of the bacterial E3s, supporting the necessary structural rearrangements associated with ubiquitin transfer. The E2-interacting surface of SopA and NleL has little similarity to those of eukaryotic E3s. However, both bacterial E3s bind to the canonical surface of E2 that normally interacts with eukaryotic E3s. Furthermore, we show that a glutamate residue on E3 is involved in catalyzing ubiquitin transfer from E3 to the substrate, but not from E2 to E3. Together, these results provide mechanistic insights into the ubiquitin pathway and a framework for understanding molecular mimicry in bacterial pathogenesis.

PubMed: 22308380
DOI: 10.1073/pnas.1115025109

Experimental method

X-RAY DIFFRACTION (3.3 Å)