5EIU

Mini TRIM5 B-box 2 dimer C2 crystal form

Summary for 5EIU

• Entry DOI: 10.2210/pdb5eiu/pdb
• Descriptor: TRIM protein-E3 ligase Chimera, ZINC ION (3 entities in total)
• Functional Keywords: tripartite motif, hiv, viral restriction, trim protein, e3 ligase, self-assembly, pattern recognition, ligase
• Biological source: Macaca mulatta (Rhesus macaque); More
• Total number of polymer chains: 2
• Total formula weight: 33211.45

Authors

Wagner, J.M.,Doss, G.,Pornillos, O. (deposition date: 2015-10-30, release date: 2016-06-15, Last modification date: 2024-03-06)

Primary citation

Wagner, J.M.,Roganowicz, M.D.,Skorupka, K.,Alam, S.L.,Christensen, D.E.,Doss, G.L.,Wan, Y.,Frank, G.A.,Ganser-Pornillos, B.K.,Sundquist, W.I.,Pornillos, O.
Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5 alpha.
Elife, 5:-, 2016

PubMed Abstract: Restriction factors and pattern recognition receptors are important components of intrinsic cellular defenses against viral infection. Mammalian TRIM5α proteins are restriction factors and receptors that target the capsid cores of retroviruses and activate ubiquitin-dependent antiviral responses upon capsid recognition. Here, we report crystallographic and functional studies of the TRIM5α B-box 2 domain, which mediates higher-order assembly of TRIM5 proteins. The B-box can form both dimers and trimers, and the trimers can link multiple TRIM5α proteins into a hexagonal net that matches the lattice arrangement of capsid subunits and enables avid capsid binding. Two modes of conformational flexibility allow TRIM5α to accommodate the variable curvature of retroviral capsids. B-box mediated interactions also modulate TRIM5α's E3 ubiquitin ligase activity, by stereochemically restricting how the N-terminal RING domain can dimerize. Overall, these studies define important molecular details of cellular recognition of retroviruses, and how recognition links to downstream processes to disable the virus.

PubMed: 27253059
DOI: 10.7554/eLife.16309

Experimental method

X-RAY DIFFRACTION (1.908 Å)