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2R15

Crystal structure of the myomesin domains 12 and 13

Summary for 2R15
Entry DOI10.2210/pdb2r15/pdb
DescriptorMyomesin-1, ACETATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordssarcomeric protein, ig-like domains, homodimer, immunoglobulin domain, muscle protein, thick filament, contractile protein
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm, myofibril, sarcomere, M line : P52179
Total number of polymer chains2
Total formula weight47091.47
Authors
Pinotsis, N.,Wilmanns, M.,Lange, S. (deposition date: 2007-08-22, release date: 2008-01-29, Last modification date: 2024-03-13)
Primary citationPinotsis, N.,Lange, S.,Perriard, J.C.,Svergun, D.I.,Wilmanns, M.
Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.
Embo J., 27:253-264, 2008
Cited by
PubMed Abstract: Sarcomeric filament proteins display extraordinary properties in terms of protein length and mechanical elasticity, requiring specific anchoring and assembly mechanisms. To establish the molecular basis of terminal filament assembly, we have selected the sarcomeric M-band protein myomesin as a prototypic filament model. The crystal structure of the myomesin C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length. Although the two domains share the same fold, an unexpected rearrangement of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two domains are connected by a six-turn alpha-helix, of which two turns are void of any interactions with other protein parts. Thus, the overall structure of the assembled myomesin C-terminus resembles a three-body beads-on-the-string model with potentially elastic properties. We predict that the found My12-helix-My13 domain topology may provide a structural template for the filament architecture of the entire C-terminal Ig domain array My9-My13 of myomesin.
PubMed: 18059477
DOI: 10.1038/sj.emboj.7601944
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.24 Å)
Structure validation

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