3B43

I-band fragment I65-I70 from titin

Summary for 3B43

• Entry DOI: 10.2210/pdb3b43/pdb
• Related: 2rik 2rjm
• Descriptor: Titin (1 entity in total)
• Functional Keywords: i-set ig fold, extended poly-ig filament, titin, elastic filament, structural protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 1
• Total formula weight: 62888.96

Authors

von Castelmur, E.,Marino, M.,Labeit, D.,Labeit, S.,Mayans, O. (deposition date: 2007-10-23, release date: 2008-01-22, Last modification date: 2024-10-30)

Primary citation

von Castelmur, E.,Marino, M.,Svergun, D.I.,Kreplak, L.,Ucurum-Fotiadis, Z.,Konarev, P.V.,Urzhumtsev, A.,Labeit, D.,Labeit, S.,Mayans, O.
A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain
Proc.Natl.Acad.Sci.Usa, 105:1186-1191, 2008

PubMed Abstract: Myofibril elasticity, critical to muscle function, is dictated by the intrasarcomeric filament titin, which acts as a molecular spring. To date, the molecular events underlying the mechanics of the folded titin chain remain largely unknown. We have elucidated the crystal structure of the 6-Ig fragment I65-I70 from the elastic I-band fraction of titin and validated its conformation in solution using small angle x-ray scattering. The long-range properties of the chain have been visualized by electron microscopy on a 19-Ig fragment and modeled for the full skeletal tandem. Results show that conserved Ig-Ig transition motifs generate high-order in the structure of the filament, where conformationally stiff segments interspersed with pliant hinges form a regular pattern of dynamic super-motifs leading to segmental flexibility in the chain. Pliant hinges support molecular shape rearrangements that dominate chain behavior at moderate stretch, whereas stiffer segments predictably oppose high stretch forces upon full chain extension. There, librational entropy can be expected to act as an energy barrier to prevent Ig unfolding while, instead, triggering the unraveling of flanking springs formed by proline, glutamate, valine, and lysine (PEVK) sequences. We propose a mechanistic model based on freely jointed rigid segments that rationalizes the response to stretch of titin Ig-tandems according to molecular features.

PubMed: 18212128
DOI: 10.1073/pnas.0707163105

Experimental method

X-RAY DIFFRACTION (3.3 Å)