SASDDD9: Cardiac myosin binding protein C: tri-helix bundle from the motif...

Basic information

• Entry: Database: SASBDB / ID: SASDDD9

Sample

Cardiac myosin binding protein C: tri-helix bundle from the motif with C2 domain

• cardiac myosin binding protein C: tri-helix bundle-C2 (protein), tri-helix bundle-C2, human sequence obtained using E. coli expression

Function / homology

Function:

C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / cardiac myofibril / regulation of striated muscle contraction / positive regulation of ATP-dependent activity / Striated Muscle Contraction / A band / structural constituent of muscle / ventricular cardiac muscle tissue morphogenesis / sarcomere organization / myosin binding / myosin heavy chain binding / ATPase activator activity / heart morphogenesis / cardiac muscle contraction / titin binding / sarcomere / actin binding / cell adhesion / identical protein binding / metal ion binding / cytosol

Domain/homology:

MyBP-C, tri-helix bundle domain / Tri-helix bundle domain / 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:

Myosin-binding protein C, cardiac-type

• Biological species: human sequence obtained using E. coli expression
• Citation: Journal: Structure / Year: 2016; Title: A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C.; Authors: Katharine A Michie / Ann H Kwan / Chang-Shung Tung / J Mitchell Guss / Jill Trewhella / ; Abstract: The nuclear magnetic resonance (NMR) structure of the tri-helix bundle (THB) of the m-domain plus C2 (ΔmC2) of myosin-binding protein C (MyBP-C) has revealed a highly flexible seven-residue linker between the structured THB and C2. Bioinformatics shows significant patterns of conservation across the THB-linker sequence, with the linker containing a strictly conserved serine in all MyBP-C isoforms. Clinically linked mutations further support the functional significance of the THB-linker region. NMR, small-angle X-ray scattering, and binding studies show the THB-linker plus the first ten residues of C2 undergo dramatic changes when ΔmC2 binds Ca-calmodulin, with the linker and C2 N-terminal residues contributing significantly to the affinity. Modeling of all available experimental data indicates that the THB tertiary structure must be disrupted to form the complex. These results are discussed in the context of the THB-linker and the N-terminal residues of C2 forming a polymorphic binding domain that could accommodate multiple binding partners in the dynamic sarcomere.

Contact author

• Jill Trewhella (School of Molecular Bioscience, University of Sydney., Sydney, New South Wales 2006, Australia)

Models

• Model #2155: ; Type: atomic / Comment: one state of 2-state MultiFoXS model, weight 0.753 / Chi-square value: 3.56671154143 / P-value: 0.820000; Search similar-shape structures of this assembly by Omokage search (details)
• Model #2156: ; Type: atomic / Comment: one state of 2-state MultiFoXS model, weight 0.247 / Chi-square value: 3.56671154143 / P-value: 0.820000; Search similar-shape structures of this assembly by Omokage search (details)

Sample

• Sample: Name: Cardiac myosin binding protein C: tri-helix bundle from the motif with C2 domain; Specimen concentration: 0.98-4.89
• Buffer: Name: 150 mM NaCl, 10 mM MES, 2 mM TCEP, 1 mM NaN3 at 4°C / pH: 6.5

Entity #1178

Name: tri-helix bundle-C2 / Type: protein
Description: cardiac myosin binding protein C: tri-helix bundle-C2
Formula weight: 15.474 / Num. of mol.: 1 / Source: human sequence obtained using E. coli expression / References: UniProt: Q14896
Sequence:

GPGSEDVWEI LRQAPPSEYE RIAFQYGVTD LRGMLKRLKG MRRDEKKSTA FQKKLEPAYQ VSKGHKIRLT VELADHDAEV KWLKNGQEIQ MSGSKYIFES IGAKRTLTIS QCSLADDAAY QCVVGGEKCS TELFVKE

Experimental information

• Beam: Instrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia / Shape: Point / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.10332 Å / Dist. spec. to detc.: 2.68024 mm
• Detector: Name: Pilatus 1M / Pixsize x: 172 mm

Scan

Title: Cardiac myosin binding protein C: tri-helix bundle from the motif with C2 domain
Measurement date: Apr 18, 2015 / Cell temperature: 22 °C / Exposure time: 1 sec. / Number of frames: 26 / Unit: 1/A /

	Min	Max
Q	0.0096	0.3436

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 733 /

	Min	Max
Q	0.0161956	0.301584
P(R) point	1	733
R	0	80

Result

Type of curve: extrapolated
Comments: The concentration series SAXS data and EOM models are provided in the full entry zip archive.

	Experimental	Standard	Porod
MW	15.475 kDa	17.896 kDa	13.067 kDa
Volume	-	-	19.6 nm3

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	0.04606	5.0E-5	0.046	0.0001
Radius of gyration, Rg	1.99 nm	0.05	1.91 nm	0.08

	Min	Max
D	-	8
Guinier point	18	146