5FM8
Structure of the C-terminally extended domain My4 of human myomesin (space group P65)
Summary for 5FM8
| Entry DOI | 10.2210/pdb5fm8/pdb |
| Related | 5FM4 5FM5 |
| Descriptor | MYOMESIN-1, NICKEL (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
| Functional Keywords | structural protein, sarcomere, m-band, fibronectin domain |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm, myofibril, sarcomere, M line : P52179 |
| Total number of polymer chains | 4 |
| Total formula weight | 48987.39 |
| Authors | Pernigo, S.,Steiner, R.A. (deposition date: 2015-11-02, release date: 2016-11-23, Last modification date: 2024-01-10) |
| Primary citation | Pernigo, S.,Fukuzawa, A.,Beedle, A.E.,Holt, M.,Round, A.,Pandini, A.,Garcia-Manyes, S.,Gautel, M.,Steiner, R.A. Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection. Structure, 25:107-120, 2017 Cited by PubMed Abstract: The sarcomeric cytoskeleton is a network of modular proteins that integrate mechanical and signaling roles. Obscurin, or its homolog obscurin-like-1, bridges the giant ruler titin and the myosin crosslinker myomesin at the M-band. Yet, the molecular mechanisms underlying the physical obscurin(-like-1):myomesin connection, important for mechanical integrity of the M-band, remained elusive. Here, using a combination of structural, cellular, and single-molecule force spectroscopy techniques, we decode the architectural and functional determinants defining the obscurin(-like-1):myomesin complex. The crystal structure reveals a trans-complementation mechanism whereby an incomplete immunoglobulin-like domain assimilates an isoform-specific myomesin interdomain sequence. Crucially, this unconventional architecture provides mechanical stability up to forces of ∼135 pN. A cellular competition assay in neonatal rat cardiomyocytes validates the complex and provides the rationale for the isoform specificity of the interaction. Altogether, our results reveal a novel binding strategy in sarcomere assembly, which might have implications on muscle nanomechanics and overall M-band organization. PubMed: 27989621DOI: 10.1016/j.str.2016.11.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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