4LTB

Coiled-coil domain of TRIM25

Summary for 4LTB

• Entry DOI: 10.2210/pdb4ltb/pdb
• Descriptor: Tripartite motif-containing 25 variant (2 entities in total)
• Functional Keywords: coiled-coil, metal binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 43743.57

Authors

Pornillos, O.,Sanchez, J.G.,Okreglicka, K. (deposition date: 2013-07-23, release date: 2014-02-05, Last modification date: 2024-02-28)

Primary citation

Sanchez, J.G.,Okreglicka, K.,Chandrasekaran, V.,Welker, J.M.,Sundquist, W.I.,Pornillos, O.
The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.
Proc.Natl.Acad.Sci.USA, 111:2494-2499, 2014

PubMed Abstract: Tripartite motif (TRIM) proteins make up a large family of coiled-coil-containing RING E3 ligases that function in many cellular processes, particularly innate antiviral response pathways. Both dimerization and higher-order assembly are important elements of TRIM protein function, but the atomic details of TRIM tertiary and quaternary structure have not been fully understood. Here, we present crystallographic and biochemical analyses of the TRIM coiled-coil and show that TRIM proteins dimerize by forming interdigitating antiparallel helical hairpins that position the N-terminal catalytic RING domains at opposite ends of the dimer and the C-terminal substrate-binding domains at the center. The dimer core comprises an antiparallel coiled-coil with a distinctive, symmetric pattern of flanking heptad and central hendecad repeats that appear to be conserved across the entire TRIM family. Our studies reveal how the coiled-coil organizes TRIM25 to polyubiquitylate the RIG-I/viral RNA recognition complex and how dimers of the TRIM5α protein are arranged within hexagonal arrays that recognize the HIV-1 capsid lattice and restrict retroviral replication.

PubMed: 24550273
DOI: 10.1073/pnas.1318962111

Experimental method

X-RAY DIFFRACTION (2.59 Å)