2F8V

Structure of full length telethonin in complex with the N-terminus of titin

Summary for 2F8V

• Entry DOI: 10.2210/pdb2f8v/pdb
• Related: 1YA5
• Descriptor: N2B-Titin Isoform, Telethonin, SULFATE ION, ... (4 entities in total)
• Functional Keywords: sarcomere, titin, z1z2, telethonin, contractile protein-contractile protein complex, contractile protein/contractile protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm (Probable): Q8WZ42; Cytoplasm, myofibril, sarcomere: O15273
• Total number of polymer chains: 6
• Total formula weight: 124798.86

Authors

Pinotsis, N.,Petoukhov, M.,Lange, S.,Svergun, D.,Zou, P.,Gautel, M.,Wilmanns, M. (deposition date: 2005-12-04, release date: 2006-06-27, Last modification date: 2023-08-30)

Primary citation

Pinotsis, N.,Petoukhov, M.,Lange, S.,Svergun, D.,Zou, P.,Gautel, M.,Wilmanns, M.
Evidence for a dimeric assembly of two titin/telethonin complexes induced by the telethonin C-terminus.
J.Struct.Biol., 155:239-250, 2006

PubMed Abstract: The Z-disk region defines the lateral boundary of the sarcomere and requires a high level of mechanical strength to provide a stable framework for large filamentous muscle proteins. The level of complexity at this area is reflected by a large number of protein-protein interactions. Recently, we unraveled how the N-terminus of the longest filament component, the giant muscle protein titin, is assembled into an antiparallel (2:1) sandwich complex by the N-terminal titin-binding segment of the Z-disk ligand telethonin/T-cap [Zou, P., Pinotsis, N., Lange, S., Song, Y.H., Popov, A., Mavridis, I., Mayans, O.M., Gautel, M., Wilmanns, M., 2006. Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk. Nature 439, 229-233]. In this contribution, we present structural data of a related complex of the titin N-terminus with full-length telethonin. The C-terminus of telethonin remains invisible, suggesting that it does not fold into a defined structure even in the presence of titin. In contrast to the structure with truncated telethonin, a dimer of two titin/telethonin complexes is formed within the crystal environment, potentially indicating the formation of higher oligomers. We further investigated the structure and dynamics of this assembly by small-angle X-ray scattering, circular dichroism, and in vivo complementation data. The data consistently indicate the involvement of the C-terminal part of telethonin into the assembly of two titin/telethonin complexes.

PubMed: 16713295
DOI: 10.1016/j.jsb.2006.03.028

Experimental method

X-RAY DIFFRACTION (2.75 Å)