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

Basic information

• Entry: Database: SASBDB / ID: SASDAK5

Sample

Myomesin-1 My12-My13

• Myomesin-1 (protein), Homo sapiens

Function / homology

Function:

extraocular skeletal muscle development / striated muscle myosin thick filament / M band / structural constituent of muscle / protein kinase A signaling / positive regulation of protein secretion / kinase binding / positive regulation of gene expression / protein homodimerization activity / identical protein binding

Domain/homology:

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

Component:

Myomesin-1

• Biological species: Homo sapiens (human)
• Citation: Journal: 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 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)

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)

Sample

• Sample: Name: Myomesin-1 My12-My13 / Sample MW: 45.88 kDa / Specimen concentration: 2.80-7.10
• Buffer: Name: 25 mM Tris/HCl / pH: 7.5 / Composition: NaCl 150.000 mM

Entity #93

Type: 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 AYFTINGVST ADSGKYGLVV KNKYGSETSD FTVSVFIPE

Experimental information

• Beam: Instrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron
• Detector: Name: MAR 345 Image Plate

Scan

Title: Myomesin C-terminus, construct My12-My13 / Measurement date: May 7, 2005 / Unit: 1/nm /

	Min	Max
Q	0.1034	4.4691

Distance distribution function P(R)

Sofotware P(R): GNOM 4.6 / Number of points: 478 /

	Min	Max
Q	0.1558	2.238
P(R) point	13	490
R	0	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.

	Experimental	Standard	Porod
MW	45.87 kDa	47 kDa	-
Volume	-	-	56 nm3

	P(R)	Guinier
Forward scattering, I0	10070	10070
Radius of gyration, Rg	4.1 nm	4 nm