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PDBsum entry 3cx2
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Contractile protein
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PDB id
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3cx2
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Contents |
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* Residue conservation analysis
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PDB id:
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Contractile protein
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Title:
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Crystal structure of the c1 domain of cardiac isoform of myosin binding protein-c at 1.3a
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Structure:
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Myosin-binding protein c, cardiac-type. Chain: a. Fragment: ig-like c2-type 1 domain. Synonym: cardiac mybp-c, c-protein, cardiac muscle isoform. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mybpc3. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.30Å
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R-factor:
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0.164
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R-free:
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0.209
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Authors:
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S.J.Fisher,J.R.Helliwell,S.Khurshid,L.Govada,C.Redwood,J.M.Squire, N.E.Chayen
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Key ref:
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S.J.Fisher
et al.
(2008).
An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C.
Acta Crystallogr D Biol Crystallogr,
64,
658-664.
PubMed id:
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Date:
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23-Apr-08
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Release date:
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01-Jul-08
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PROCHECK
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Headers
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References
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Q14896
(MYPC3_HUMAN) -
Myosin-binding protein C, cardiac-type from Homo sapiens
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Seq:
Struc:
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1274 a.a.
107 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Acta Crystallogr D Biol Crystallogr
64:658-664
(2008)
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PubMed id:
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An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C.
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S.J.Fisher,
J.R.Helliwell,
S.Khurshid,
L.Govada,
C.Redwood,
J.M.Squire,
N.E.Chayen.
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ABSTRACT
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Myosin-binding protein C (MyBP-C) is a myofibril-associated protein found in
cardiac and skeletal muscle. The cardiac isoform (cMyBP-C) is subject to
reversible phosphorylation and the surface-charge state of the protein is of
keen interest with regard to understanding the inter-protein interactions that
are implicated in its function. Diffraction data from the C1 domain of cMyBP-C
were extended to 1.30 A resolution, where the <I/sigma(I)> of the
diffraction data crosses 2.0, using intense synchrotron radiation. The
protonation-state determinations were not above 2sigma (the best was 1.81sigma)
and therefore an extrapolation is given, based on 100% data completeness and the
average DPI, that a 3sigma determination could be possible if X-ray data could
be measured to 1.02 A resolution. This might be possible via improved
crystallization or multiple sample evaluation, e.g. using robotics or a yet more
intense/collimated X-ray beam or combinations thereof. An alternative would be
neutron protein crystallography at 2 A resolution, where it is estimated that
for the unit-cell volume of the cMyBP-C C1 domain crystal a crystal volume of
0.10 mm3 would be needed with fully deuterated protein on LADI III. These
efforts would optimally be combined in a joint X-ray and neutron model
refinement.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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E.Oksanen,
M.P.Blakeley,
F.Bonneté,
M.T.Dauvergne,
F.Dauvergne,
and
M.Budayova-Spano
(2009).
Large crystal growth by thermal control allows combined X-ray and neutron crystallographic studies to elucidate the protonation states in Aspergillus flavus urate oxidase.
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J R Soc Interface,
6,
S599-S610.
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A.Ababou,
E.Rostkova,
S.Mistry,
C.Le Masurier,
M.Gautel,
and
M.Pfuhl
(2008).
Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1.
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J Mol Biol,
384,
615-630.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
