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- SASDAK5: Myomesin-1 My12-My13 (Myomesin-1) -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDAK5
SampleMyomesin-1 My12-My13
  • Myomesin-1 (protein), Homo sapiens
Function / homology
Function and homology information


extraocular skeletal muscle development / striated muscle myosin thick filament / : / M band / structural constituent of muscle / sarcomere organization / positive regulation of protein secretion / kinase binding / positive regulation of gene expression / protein homodimerization activity / identical protein binding
Similarity search - Function
: / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily ...: / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationJournal: EMBO J / Year: 2008
Title: Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.
Authors: Nikos Pinotsis / Stephan Lange / Jean-Claude Perriard / Dmitri I Svergun / Matthias Wilmanns /
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 ...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.
Contact author
  • Dmitri Svergun (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #121
Type: atomic / Software: CRYSOL / Chi-square value: 2.524921
Search similar-shape structures of this assembly by Omokage search (details)
Model #122
Type: atomic / Software: CRYSOL / Chi-square value: 8.2944
Search similar-shape structures of this assembly by Omokage search (details)
Model #123
Type: atomic / Software: CRYSOL / Chi-square value: 64.416676
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Myomesin-1 My12-My13 / Sample MW: 45.88 kDa / Specimen concentration: 2.80-7.10
BufferName: 25 mM Tris/HCl / pH: 7.5 / Composition: NaCl 150.000 mM
Entity #93Type: protein / Description: Myomesin-1 / Formula weight: 22.94 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: P52179
Sequence: IALSATDLKI QSTAEGIQLY SFVTYYVEDL KVNWSHNGSA IRYSDRVKTG VTGEQIWLQI NEPTPNDKGK YVMELFDGKT GHQKTVDLSG QAYDEAYAEF QRLKQAAIAE KNRARVLGGL PDVVTIQEGK ALNLTCNVWG DPPPEVSWLK NEKALASDDH CNLKFEAGRT ...Sequence:
IALSATDLKI QSTAEGIQLY SFVTYYVEDL KVNWSHNGSA IRYSDRVKTG VTGEQIWLQI NEPTPNDKGK YVMELFDGKT GHQKTVDLSG QAYDEAYAEF QRLKQAAIAE KNRARVLGGL PDVVTIQEGK ALNLTCNVWG DPPPEVSWLK NEKALASDDH CNLKFEAGRT AYFTINGVST ADSGKYGLVV KNKYGSETSD FTVSVFIPE

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Experimental information

BeamInstrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron
DetectorName: MAR 345 Image Plate
Scan
Title: Myomesin C-terminus, construct My12-My13 / Measurement date: May 7, 2005 / Unit: 1/nm /
MinMax
Q0.1034 4.4691
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 478 /
MinMax
Q0.1558 2.238
P(R) point13 490
R0 14.49
Result
D max: 14.5 / Type of curve: merged / Standard: BSA
Comments: Use of SAXS to discriminate between different crystallographic dimers of the C-terminal construct of myomesin-1 containing two IG-like domains.
ExperimentalStandardPorod
MW45.87 kDa47 kDa-
Volume--56 nm3

P(R)Guinier
Forward scattering, I010070 10070
Radius of gyration, Rg4.1 nm4 nm

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