3DDT

Crystal structure of the B2 box from MuRF1 in dimeric state

Summary for 3DDT

• Entry DOI: 10.2210/pdb3ddt/pdb
• Descriptor: E3 ubiquitin-protein ligase TRIM63, ZINC ION (3 entities in total)
• Functional Keywords: zinc-binding motif, ring-like fold, coiled coil, cytoplasm, ligase, metal-binding, muscle protein, nucleus, polymorphism, ubl conjugation pathway, zinc, zinc-finger
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q969Q1
• Total number of polymer chains: 3
• Total formula weight: 16224.08

Authors

Mayans, O.,Mrosek, M. (deposition date: 2008-06-06, release date: 2008-10-07, Last modification date: 2024-03-20)

Primary citation

Mrosek, M.,Meier, S.,Ucurum-Fotiadis, Z.,von Castelmur, E.,Hedbom, E.,Lustig, A.,Grzesiek, S.,Labeit, D.,Labeit, S.,Mayans, O.
Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold
Biochemistry, 47:10722-10730, 2008

PubMed Abstract: The B-box motif is the defining feature of the TRIM family of proteins, characterized by a RING finger-B-box-coiled coil tripartite fold. We have elucidated the crystal structure of B-box 2 (B2) from MuRF1, a TRIM protein that supports a wide variety of protein interactions in the sarcomere and regulates the trophic state of striated muscle tissue. MuRF1 B2 coordinates two zinc ions through a cross-brace alpha/beta-topology typical of members of the RING finger superfamily. However, it self-associates into dimers with high affinity. The dimerization pattern is mediated by the helical component of this fold and is unique among RING-like folds. This B2 reveals a long shallow groove that encircles the C-terminal metal binding site ZnII and appears as the defining protein-protein interaction feature of this domain. A cluster of conserved hydrophobic residues in this groove and, in particular, a highly conserved aromatic residue (Y133 in MuRF1 B2) is likely to be central to this role. We expect these findings to aid the future exploration of the cellular function and therapeutic potential of MuRF1.

PubMed: 18795805
DOI: 10.1021/bi800733z

Experimental method

X-RAY DIFFRACTION (1.9 Å)