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PDBsum entry 4tnc

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protein metals links
Contractile system protein PDB id
4tnc
Jmol
Contents
Protein chain
160 a.a. *
Metals
_CA ×2
Waters ×68
* Residue conservation analysis
PDB id:
4tnc
Name: Contractile system protein
Title: Refined structure of chicken skeletal muscle troponin c in the two-calcium state at 2-angstroms resolution
Structure: Troponin c. Chain: a. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031
Resolution:
2.00Å     R-factor:   0.172    
Authors: M.Sundaralingam
Key ref: K.A.Satyshur et al. (1988). Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution. J Biol Chem, 263, 1628-1647. PubMed id: 3338985
Date:
28-Sep-87     Release date:   16-Jul-88    
Supersedes: 3tnc
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02588  (TNNC2_CHICK) -  Troponin C, skeletal muscle
Seq:
Struc:
163 a.a.
160 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     troponin complex   1 term 
  Biological process     skeletal muscle contraction   1 term 
  Biochemical function     actin binding     3 terms  

 

 
J Biol Chem 263:1628-1647 (1988)
PubMed id: 3338985  
 
 
Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution.
K.A.Satyshur, S.T.Rao, D.Pyzalska, W.Drendel, M.Greaser, M.Sundaralingam.
 
  ABSTRACT  
 
The structure of troponin C has been refined at 2A resolution to an R value of 0.172 using a total of 8,100 reflections. Troponin C has an unusual dumbbell shape with only the two C-domain high affinity sites III and IV occupied with metals, while the pair of N-domain low affinity sites I and II are devoid of metals. The coordination of the Ca2+ approaches seven with the last glutamic acid residue in each site forming an asymmetric bidentate ligand. The flanking helices in the metal-bound EF hands are in similar orientation (both 113 degrees) while in the apo sites they are more obtuse (134 and 149 degrees). The EF hands of holo sites III and IV are similar while the apo sites I and II are less similar (rms for backbone atoms, 0.78 and 1.44). The half-loops of the 12-residue holo and apo sites show better agreement than the full loops themselves, suggesting a hinge motion at the midpoint of the loops. The long central helix is stabilized by electrostatic interactions and salt bridges between charged side chains spaced at 3 or 4 residues along the helix. A cluster of water molecules encircle the long helix and hydrogen bond to the backbone carbonyls. At the beginning of the B-helix, a water molecule is interposed at each of two consecutive backbone NH...OC hydrogen bonds. The terminal pair of helices A/D (apo) match with E/H (holo), and the internal pair of helices B/C (apo) match with F/G (holo). Thus, muscle contraction may be triggered by Ca2+ binding to loops I and II which results in a concerted rearrangement of residues in the loops, including the essential Gly at position 6 in each loop. This rearrangement than causes a reorientation of helices B and C along with the BC linker.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19437460 D.J.Muehsam, and A.A.Pilla (2009).
A Lorentz model for weak magnetic field bioeffects: part I--thermal noise is an essential component of AC/DC effects on bound ion trajectory.
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19321741 G.Neti, S.M.Novak, V.F.Thompson, and D.E.Goll (2009).
Properties of easily releasable myofilaments: are they the first step in myofibrillar protein turnover?
  Am J Physiol Cell Physiol, 296, C1383-C1390.  
19542563 I.M.Robertson, M.X.Li, and B.D.Sykes (2009).
Solution structure of human cardiac troponin C in complex with the green tea polyphenol, (-)-epigallocatechin 3-gallate.
  J Biol Chem, 284, 23012-23023.
PDB code: 2kdh
19439414 J.R.Pinto, M.S.Parvatiyar, M.A.Jones, J.Liang, M.J.Ackerman, and J.D.Potter (2009).
A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy.
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15784741 M.V.Vinogradova, D.B.Stone, G.G.Malanina, C.Karatzaferi, R.Cooke, R.A.Mendelson, and R.J.Fletterick (2005).
Ca(2+)-regulated structural changes in troponin.
  Proc Natl Acad Sci U S A, 102, 5038-5043.
PDB codes: 1ytz 1yv0
11943596 E.F.da Silva, V.H.Oliveira, M.M.Sorenson, H.Barrabin, and H.M.Scofano (2002).
Converting troponin C into calmodulin: effects of mutations in the central helix and of changes in temperature.
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12239350 L.J.Brown, K.L.Sale, R.Hills, C.Rouviere, L.Song, X.Zhang, and P.G.Fajer (2002).
Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance.
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12022873 S.B.Tikunova, J.A.Rall, and J.P.Davis (2002).
Effect of hydrophobic residue substitutions with glutamine on Ca(2+) binding and exchange with the N-domain of troponin C.
  Biochemistry, 41, 6697-6705.  
11705966 G.D.Pullinger, R.Sowdhamini, and A.J.Lax (2001).
Localization of functional domains of the mitogenic toxin of Pasteurella multocida.
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11180252 V.N.Binhi, Y.D.Alipov, and I.Y.Belyaev (2001).
Effect of static magnetic field on E. coli cells and individual rotations of ion-protein complexes.
  Bioelectromagnetics, 22, 79-86.  
  10933496 C.S.Tung, M.E.Wall, S.C.Gallagher, and J.Trewhella (2000).
A model of troponin-I in complex with troponin-C using hybrid experimental data: the inhibitory region is a beta-hairpin.
  Protein Sci, 9, 1312-1326.
PDB code: 1ew7
10747786 J.K.Krueger, S.C.Gallagher, C.A.Wang, and J.Trewhella (2000).
Calmodulin remains extended upon binding to smooth muscle caldesmon: a combined small-angle scattering and fourier transform infrared spectroscopy study.
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11054120 K.Pääkkönen, T.Sorsa, T.Drakenberg, P.Pollesello, C.Tilgmann, P.Permi, S.Heikkinen, I.Kilpeläinen, and A.Annila (2000).
Conformations of the regulatory domain of cardiac troponin C examined by residual dipolar couplings.
  Eur J Biochem, 267, 6665-6672.  
10715110 P.Mercier, M.X.Li, and B.D.Sykes (2000).
Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I.
  Biochemistry, 39, 2902-2911.  
10615090 V.N.Binhi (2000).
Amplitude and frequency dissociation spectra of ion-protein complexes rotating in magnetic fields.
  Bioelectromagnetics, 21, 34-45.  
10792039 Y.Li, M.L.Love, J.A.Putkey, and C.Cohen (2000).
Bepridil opens the regulatory N-terminal lobe of cardiac troponin C.
  Proc Natl Acad Sci U S A, 97, 5140-5145.
PDB code: 1dtl
9876151 L.Smith, N.J.Greenfield, and S.E.Hitchcock-DeGregori (1999).
Mutations in the N- and D-helices of the N-domain of troponin C affect the C-domain and regulatory function.
  Biophys J, 76, 400-408.  
10387074 M.X.Li, L.Spyracopoulos, and B.D.Sykes (1999).
Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C.
  Biochemistry, 38, 8289-8298.
PDB code: 1mxl
10220335 R.T.McKay, B.P.Tripet, J.R.Pearlstone, L.B.Smillie, and B.D.Sykes (1999).
Defining the region of troponin-I that binds to troponin-C.
  Biochemistry, 38, 5478-5489.  
10231519 S.Tsuda, A.Miura, S.M.Gagné, L.Spyracopoulos, and B.D.Sykes (1999).
Low-temperature-induced structural changes in the Apo regulatory domain of skeletal muscle troponin C.
  Biochemistry, 38, 5693-5700.
PDB codes: 1skt 1zac
  9828012 A.L.Hazard, S.C.Kohout, N.L.Stricker, J.A.Putkey, and J.J.Falke (1998).
The kinetic cycle of cardiac troponin C: calcium binding and dissociation at site II trigger slow conformational rearrangements.
  Protein Sci, 7, 2451-2459.  
9922172 L.Spyracopoulos, S.M.Gagné, M.X.Li, and B.D.Sykes (1998).
Dynamics and thermodynamics of the regulatory domain of human cardiac troponin C in the apo- and calcium-saturated states.
  Biochemistry, 37, 18032-18044.  
9730814 R.T.McKay, J.R.Pearlstone, D.C.Corson, S.M.Gagné, L.B.Smillie, and B.D.Sykes (1998).
Structure and interaction site of the regulatory domain of troponin-C when complexed with the 96-148 region of troponin-I.
  Biochemistry, 37, 12419-12430.
PDB code: 1blq
9519411 S.P.Smith, and G.S.Shaw (1998).
A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.
  Structure, 6, 211-222.
PDB code: 1uwo
9199794 D.R.Swartz, R.L.Moss, and M.L.Greaser (1997).
Characteristics of troponin C binding to the myofibrillar thin filament: extraction of troponin C is not random along the length of the thin filament.
  Biophys J, 73, 293-305.  
9122189 J.Zhou, R.Olcese, N.Qin, F.Noceti, L.Birnbaumer, and E.Stefani (1997).
Feedback inhibition of Ca2+ channels by Ca2+ depends on a short sequence of the C terminus that does not include the Ca2+ -binding function of a motif with similarity to Ca2+ -binding domains.
  Proc Natl Acad Sci U S A, 94, 2301-2305.  
9315850 L.Spyracopoulos, M.X.Li, S.K.Sia, S.M.Gagné, M.Chandra, R.J.Solaro, and B.D.Sykes (1997).
Calcium-induced structural transition in the regulatory domain of human cardiac troponin C.
  Biochemistry, 36, 12138-12146.
PDB codes: 1ap4 1spy
  9385641 S.Linse, E.Thulin, L.K.Gifford, D.Radzewsky, J.Hagan, R.R.Wilk, and K.S.Akerfeldt (1997).
Domain organization of calbindin D28k as determined from the association of six synthetic EF-hand fragments.
  Protein Sci, 6, 2385-2396.  
9109645 S.M.Gagné, M.X.Li, and B.D.Sykes (1997).
Mechanism of direct coupling between binding and induced structural change in regulatory calcium binding proteins.
  Biochemistry, 36, 4386-4392.
PDB code: 1smg
9017210 W.J.Dong, C.K.Wang, A.M.Gordon, and H.C.Cheung (1997).
Disparate fluorescence properties of 2-[4'-(iodoacetamido)anilino]-naphthalene-6-sulfonic acid attached to Cys-84 and Cys-35 of troponin C in cardiac muscle troponin.
  Biophys J, 72, 850-857.  
8994973 A.Houdusse, M.Silver, and C.Cohen (1996).
A model of Ca(2+)-free calmodulin binding to unconventional myosins reveals how calmodulin acts as a regulatory switch.
  Structure, 4, 1475-1490.
PDB code: 1aji
8855232 D.Foguel, M.C.Suarez, C.Barbosa, J.J.Rodrigues, M.M.Sorenson, L.B.Smillie, and J.L.Silva (1996).
Mimicry of the calcium-induced conformational state of troponin C by low temperature under pressure.
  Proc Natl Acad Sci U S A, 93, 10642-10646.  
8652520 G.S.Shaw, and B.D.Sykes (1996).
NMR solution structure of a synthetic troponin C heterodimeric domain.
  Biochemistry, 35, 7429-7438.
PDB code: 1pon
8619985 K.S.Akerfeldt, A.N.Coyne, R.R.Wilk, E.Thulin, and S.Linse (1996).
Ca2+-binding stoichiometry of calbindin D28k as assessed by spectroscopic analyses of synthetic peptide fragments.
  Biochemistry, 35, 3662-3669.  
8874031 S.Kumar, and M.Bansal (1996).
Structural and sequence characteristics of long alpha helices in globular proteins.
  Biophys J, 71, 1574-1586.  
8688416 S.P.Smith, K.R.Barber, S.D.Dunn, and G.S.Shaw (1996).
Structural influence of cation binding to recombinant human brain S100b: evidence for calcium-induced exposure of a hydrophobic surface.
  Biochemistry, 35, 8805-8814.  
8952505 S.Ramakrishnan, and S.E.Hitchcock-DeGregori (1996).
Structural and functional significance of aspartic acid 89 of the troponin C central helix in Ca2+ signaling.
  Biochemistry, 35, 15515-15521.  
8672440 Y.Yamazaki, S.Tuzi, H.Saitô, H.Kandori, R.Needleman, J.K.Lanyi, and A.Maeda (1996).
Hydrogen bonds of water and C==O groups coordinate long-range structural changes in the L photointermediate of bacteriorhodopsin.
  Biochemistry, 35, 4063-4068.  
  7613474 C.Donaldson, K.R.Barber, C.M.Kay, and G.S.Shaw (1995).
Human S100b protein: formation of a tetramer from synthetic calcium-binding site peptides.
  Protein Sci, 4, 765-772.  
  7670371 C.M.Slupsky, F.C.Reinach, L.B.Smillie, and B.D.Sykes (1995).
Solution secondary structure of calcium-saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy.
  Protein Sci, 4, 1279-1290.  
  7613465 J.W.Howarth, G.A.Krudy, X.Lin, J.A.Putkey, and P.R.Rosevear (1995).
An NMR and spin label study of the effects of binding calcium and troponin I inhibitory peptide to cardiac troponin C.
  Protein Sci, 4, 671-680.  
8569721 K.Balendiran, Y.Tan, R.K.Sharma, and K.H.Murthy (1995).
Preliminary crystallization studies of calmodulin-dependent protein phosphatase (calcineurin) from bovine brain.
  Mol Cell Biochem, 149, 127-130.  
7552750 S.M.Gagné, S.Tsuda, M.X.Li, L.B.Smillie, and B.D.Sykes (1995).
Structures of the troponin C regulatory domains in the apo and calcium-saturated states.
  Nat Struct Biol, 2, 784-789.
PDB codes: 1tnp 1tnq
7552734 W.J.Chazin (1995).
Releasing the calcium trigger.
  Nat Struct Biol, 2, 707-710.  
  7920247 G.S.Shaw, R.S.Hodges, C.M.Kay, and B.D.Sykes (1994).
Relative stabilities of synthetic peptide homo- and heterodimeric troponin-C domains.
  Protein Sci, 3, 1010-1019.  
7922316 J.F.Head (1994).
Phototransduction. Shedding light on recoverin.
  Curr Biol, 4, 64-66.  
7899550 J.J.Falke, S.K.Drake, A.L.Hazard, and O.B.Peersen (1994).
Molecular tuning of ion binding to calcium signaling proteins.
  Q Rev Biophys, 27, 219-290.  
  8003981 J.R.Lakowicz, I.Gryczynski, G.Laczko, W.Wiczk, and M.L.Johnson (1994).
Distribution of distances between the tryptophan and the N-terminal residue of melittin in its complex with calmodulin, troponin C, and phospholipids.
  Protein Sci, 3, 628-637.  
  7703843 S.M.Gagné, S.Tsuda, M.X.Li, M.Chandra, L.B.Smillie, and B.D.Sykes (1994).
Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C.
  Protein Sci, 3, 1961-1974.  
8168542 T.Takagi, T.Petrova, M.Comte, T.Kuster, C.W.Heizmann, and J.A.Cox (1994).
Characterization and primary structure of amphioxus troponin C.
  Eur J Biochem, 221, 537-546.  
8477730 A.C.da Silva, A.H.de Araujo, O.Herzberg, J.Moult, M.Sorenson, and F.C.Reinach (1993).
Troponin-C mutants with increased calcium affinity.
  Eur J Biochem, 213, 599-604.  
  8518733 C.Y.Sekharudu, and M.Sundaralingam (1993).
A model for the calmodulin-peptide complex based on the troponin C crystal packing and its similarity to the NMR structure of the calmodulin-myosin light chain kinase peptide complex.
  Protein Sci, 2, 620-625.  
  8318894 D.P.Yee, and K.A.Dill (1993).
Families and the structural relatedness among globular proteins.
  Protein Sci, 2, 884-899.  
8324198 J.D.Hannon, P.B.Chase, D.A.Martyn, L.L.Huntsman, M.J.Kushmerick, and A.M.Gordon (1993).
Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac troponin C.
  Biophys J, 64, 1632-1637.  
8136020 M.E.Huque, and H.J.Vogel (1993).
Carbon-13 NMR studies of the lysine side chains of calmodulin and its proteolytic fragments.
  J Protein Chem, 12, 695-707.  
8394001 M.H.Zehfus (1993).
Improved calculations of compactness and a reevaluation of continuous compact units.
  Proteins, 16, 293-300.  
8318669 S.G.Jacchieri, and N.G.Richards (1993).
Probing the influence of sequence-dependent interactions upon alpha-helix stability in alanine-based linear peptides.
  Biopolymers, 33, 971-984.  
8341712 S.Raghunathan, R.J.Chandross, B.P.Cheng, A.Persechini, S.E.Sobottka, and R.H.Kretsinger (1993).
The linker of des-Glu84-calmodulin is bent.
  Proc Natl Acad Sci U S A, 90, 6869-6873.
PDB code: 1deg
  8453381 S.T.Rao, S.Wu, K.A.Satyshur, K.Y.Ling, C.Kung, and M.Sundaralingam (1993).
Structure of Paramecium tetraurelia calmodulin at 1.8 A resolution.
  Protein Sci, 2, 436-447.
PDB code: 1clm
  1304891 C.M.Slupsky, G.S.Shaw, A.P.Campbell, and B.D.Sykes (1992).
A 1H NMR study of a ternary peptide complex that mimics the interaction between troponin C and troponin I.
  Protein Sci, 1, 1595-1603.  
1315966 K.Y.Ling, R.R.Preston, R.Burns, J.A.Kink, Y.Saimi, and C.Kung (1992).
Primary mutations in calmodulin prevent activation of the Ca(++)-dependent Na+ channel in Paramecium.
  Proteins, 12, 365-371.  
  1304377 O.D.Monera, G.S.Shaw, B.Y.Zhu, B.D.Sykes, C.M.Kay, and R.S.Hodges (1992).
Role of interchain alpha-helical hydrophobic interactions in Ca2+ affinity, formation, and stability of a two-site domain in troponin C.
  Protein Sci, 1, 945-955.  
1401036 Z.Grabarek, T.Tao, and J.Gergely (1992).
Molecular mechanism of troponin-C function.
  J Muscle Res Cell Motil, 13, 383-393.  
2062825 A.G.Tomasselli, W.J.Howe, J.O.Hui, T.K.Sawyer, I.M.Reardon, D.L.DeCamp, C.S.Craik, and R.L.Heinrikson (1991).
Calcium-free calmodulin is a substrate of proteases from human immunodeficiency viruses 1 and 2.
  Proteins, 10, 1-9.  
2047521 C.C.Ashley, I.P.Mulligan, and T.J.Lea (1991).
Ca2+ and activation mechanisms in skeletal muscle.
  Q Rev Biophys, 24, 1.  
2050809 J.H.Collins (1991).
Myosin light chains and troponin C: structural and evolutionary relationships revealed by amino acid sequence comparisons.
  J Muscle Res Cell Motil, 12, 3.  
1850620 L.A.Luck, and J.J.Falke (1991).
19F NMR studies of the D-galactose chemosensory receptor. 2. Ca(II) binding yields a local structural change.
  Biochemistry, 30, 4257-4261.  
1946346 M.Ovaska, and J.Taskinen (1991).
A model for human cardiac troponin C and for modulation of its Ca2+ affinity by drugs.
  Proteins, 11, 79-94.  
1791194 T.Kobayashi, H.G.Zot, T.D.Pollard, and J.H.Collins (1991).
Functional implications of the unusual amino acid sequence of the regulatory light chain of Acanthamoeba castellanii myosin-II.
  J Muscle Res Cell Motil, 12, 553-559.  
2162201 E.E.Snyder, B.W.Buoscio, and J.J.Falke (1990).
Calcium(II) site specificity: effect of size and charge on metal ion binding to an EF-hand-like site.
  Biochemistry, 29, 3937-3943.  
2351140 H.D.Schulzki, B.Kramer, J.Fleischhauer, D.A.Mercola, and A.Wollmer (1990).
Calcium-dependent distance changes in binary and ternary complexes of troponin.
  Eur J Biochem, 189, 683-692.  
2108018 K.F.Chan, and W.H.Chen (1990).
High performance capillary electrophoresis of calmodulin.
  Electrophoresis, 11, 15-18.  
2186281 K.Fujimori, M.Sorenson, O.Herzberg, J.Moult, and F.C.Reinach (1990).
Probing the calcium-induced conformational transition of troponin C with site-directed mutants.
  Nature, 345, 182-184.  
2377604 M.M.Yamashita, L.Wesson, G.Eisenman, and D.Eisenberg (1990).
Where metal ions bind in proteins.
  Proc Natl Acad Sci U S A, 87, 5648-5652.  
2115931 N.D.Moncrief, R.H.Kretsinger, and M.Goodman (1990).
Evolution of EF-hand calcium-modulated proteins. I. Relationships based on amino acid sequences.
  J Mol Evol, 30, 522-562.  
2148867 S.H.Chao, C.H.Bu, and W.Y.Cheung (1990).
Activation of troponin C by Cd2+ and Pb2+.
  Arch Toxicol, 64, 490-496.  
2110625 Z.Grabarek, R.Y.Tan, J.Wang, T.Tao, and J.Gergely (1990).
Inhibition of mutant troponin C activity by an intra-domain disulphide bond.
  Nature, 345, 132-135.  
2622912 C.K.Wang, J.Lebowitz, and H.C.Cheung (1989).
Acid-induced dimerization of skeletal troponin C.
  Proteins, 6, 424-430.  
2706314 I.L.Karle, J.L.Flippen-Anderson, K.Uma, and P.Balaram (1989).
Solvated helical backbones: x-ray diffraction study of Boc-Ala-Leu-Aib-Ala-Leu-Aib-OMe.H2O.
  Biopolymers, 28, 773-781.  
2684418 S.E.Hitchcock-DeGregori (1989).
Structure-function analysis of thin filament proteins expressed in Escherichia coli.
  Cell Motil Cytoskeleton, 14, 12-20.  
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.