1YA5

Crystal structure of the titin domains z1z2 in complex with telethonin

Summary for 1YA5

• Entry DOI: 10.2210/pdb1ya5/pdb
• Descriptor: N2B-TITIN ISOFORM, TELETHONIN, SULFATE ION, ... (4 entities in total)
• Functional Keywords: telethonin; t-cap; ig-like domains; z1; z2; titin, structural protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm, myofibril, sarcomere: O15273
• Total number of polymer chains: 3
• Total formula weight: 54266.00

Authors

Pinotsis, N.,Popov, A.,Zou, P.,Wilmanns, M. (deposition date: 2004-12-17, release date: 2005-12-20, Last modification date: 2024-02-14)

Primary citation

Zou, P.,Pinotsis, N.,Lange, S.,Song, Y.H.,Popov, A.,Mavridis, I.,Mayans, O.M.,Gautel, M.,Wilmanns, M.
Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk
Nature, 439:229-233, 2006

PubMed Abstract: The Z-disk of striated and cardiac muscle sarcomeres is one of the most densely packed cellular structures in eukaryotic cells. It provides the architectural framework for assembling and anchoring the largest known muscle filament systems by an extensive network of protein-protein interactions, requiring an extraordinary level of mechanical stability. Here we show, using X-ray crystallography, how the amino terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the Z-disk ligand telethonin. The pseudosymmetric structure of telethonin mediates a unique palindromic arrangement of two titin filaments, a type of molecular assembly previously found only in protein-DNA complexes. We have confirmed its unique architecture in vivo by protein complementation assays, and in vitro by experiments using fluorescence resonance energy transfer. The model proposed may provide a molecular paradigm of how major sarcomeric filaments are crosslinked, anchored and aligned within complex cytoskeletal networks.

PubMed: 16407954
DOI: 10.1038/nature04343

Experimental method

X-RAY DIFFRACTION (2.445 Å)