Refined crystal structure of troponin C from turkey skeletal muscle at 2·0 Å resolution

Herzberg, Osnat; James, Michael N.G.

doi:10.1016/0022-2836(88)90208-2

Cited by 337 publications

(266 citation statements)

References 34 publications

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“…The @-sheets are in an antiparallel conformation (36-38 is antiparallel to 72-74, and 112-1 14 is antiparallel to 148-150) as observed by the presence of d,,, dNN, and doN NOEs across the @-sheet (daa for D36-D74, S38-T72 [these ' H a resonances overlap], F112-DI50, and D114-Rl48; dNN for 137-173 and I1 13-1149; and dBN for 137-173 and I 1 13-I149), as was also observed for the symmetric homodimers in solution (Shaw et al, 1990;Kay et al, 1991). The calcium binding loops are well characterized by X-ray crystallographic studies (Herzberg & James, 1988;Satyshur et al, 1988Satyshur et al, , 1994 There are four connecting loops in calcium-saturated TnC.…”

Section: Secondary Structure Determinationmentioning

confidence: 57%

“…The helices were thus broken up at R84 and restarted at D89. The crystal structure of half-saturated TnC reveals similar starts and stops of helices (Herzberg & James, 1988;Satyshur et al, 1988Satyshur et al, , 1994 except for the ends of some helices and in the linker region between the two domains where the helix is contiguous in the crystal structure (from F75 to F105). One residue of particular interest, is the residue Glu 41.…”

Section: Secondary Structure Determinationmentioning

confidence: 97%

“…Chicken skeletal TnC has 162 amino acid residues (for a molecular weight of 18,257) and binds four metal ions in four separate metal ionbinding sites numbered consecutively from the N-terminus of the protein. The structure of half-saturated avian skeletal TnC (with calcium binding sites 111 and IV filled) has been solved using X-ray crystallographic techniques (Herzberg & James, 1988;Satyshur et al, 1988Satyshur et al, , 1994 and reveals two domains (the C-terminal and the N-terminal domains), each with two EF-hand helix-loop-helix calcium binding sites. The C-terminal domain contains the high affinity calcium/magnesium binding sites, which have a Kc, in the range of 2 X IO' M" ; these are referred to as the structural sites because they are always filled with calcium or magnesium in the muscle cell (Potter & Gergely, 1975).…”

Section: ~mentioning

confidence: 99%

“…One residue of particular interest, is the residue Glu 41. This residue was found to have "irregular" non- F22 K23 A24 A25 F26 D27 M28 F29 D30 A3 1 D32 G33 G34 G35 D36 137 S38 T39 K40 E4 1 L42 G43 "44 v45 M46 R47 M48 L49 G50 Q5 1 N52 P53 T54 K55 E56 E57 L58 D59 helical $/$ angles (4 = -96"; $ = -7') in the crystal structure and was shown to form a "kink" in helix B of the crystal structure where the N-domains are free of calcium (Herzberg & James, 1988;Satyshur et al, 1988Satyshur et al, , 1994. The calcium-saturated TnC structure presented here has no indication of $/$ angles for residue Glu 41 other than helix, suggesting that this residue has shifted its $/$ angles to better fit into a helix in the calciumsaturated form.…”

Section: Secondary Structure Determinationmentioning

confidence: 99%

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Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy

et al. 1995

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The solution secondary structure of calcium-saturated skeletal troponin C (TnC) in the presence of 15% (v/v) trifluoroethanol (TFE), which has been shown to exist predominantly as a monomer (Slupsky CM, Kay CM, Reinach FC, Smillie LB, Sykes BD, 1995, Biochemistry 34, forthcoming), has been investigated using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The ' H , I5N, and I3C NMR chemical shift values for TnC in the presence of TFE are very similar to values obtained for calcium-saturated NTnC (residues 1-90 of skeletal TnC), calmodulin, and synthetic peptide homodimers. Moreover, the secondary structure elements of TnC are virtually identical to those obtained for calcium-saturated NTnC, calmodulin, and the synthetic peptide homodimers, suggesting that 15% (v/v) TFE minimally perturbs the secondary and tertiary structure of this stably folded protein. Comparison of the solution structure of calcium-saturated TnC with the X-ray crystal structure of half-saturated TnC reveals differences in the 414 angles of residue Glu 41 and in the linker between the two domains. Glu 41 has irregular 4/$ angles in the crystal structure, producing a kink in the B helix, whereas in calciumsaturated TnC, Glu 41 has helical +/$ angles, resulting in a straight B helix. The linker between the N and C domains of calcium-saturated TnC is flexible in the solution structure.

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Section: Secondary Structure Determinationmentioning

confidence: 57%

Section: Secondary Structure Determinationmentioning

confidence: 97%

Section: ~mentioning

confidence: 99%

Section: Secondary Structure Determinationmentioning

confidence: 99%

See 2 more Smart Citations

Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy

et al. 1995

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“…Analysis of the contrast dependence of the R g values from the complex revealed that the centers of mass of the two components are coincident. Using a Monte Carlo modeling approach, together with the available crystal structure of 2Ca 21 Á sTnC, 29,47 Olah and Trewhella 48 generated a model for the skeletal 4Ca 21 Á sTnC-sTnI complex. In the crystal structure of 2Ca 21 Á sTnC, only the highaffinity Ca 21 binding sites at the C-terminal domain are occupied and to best-fit the scattering data, it was necessary to modify the N-terminal domain in the crystal structure to be more open, mimicking the Ca 21 bound C-terminal domain.…”

Section: Skeletal and Cardiac Isoforms Of Troponinmentioning

confidence: 99%

Invited review: Probing the structures of muscle regulatory proteins using small‐angle solution scattering

Jeffries

Trewhella

2011

Biopolymers

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Small‐angle X‐ray and neutron scattering with contrast variation have made important contributions in advancing our understanding of muscle regulatory protein structures in the context of the dynamic molecular processes governing muscle action. The contributions of the scattering investigations have depended upon the results of key crystallographic, NMR, and electron microscopy experiments that have provided detailed structural information that has aided in the interpretation of the scattering data. This review will cover the advances made using small‐angle scattering techniques, in combination with the results from these complementary techniques, in probing the structures of troponin and myosin binding protein C. A focus of the troponin work has been to understand the isoform differences between the skeletal and cardiac isoforms of this major calcium receptor in muscle. In the case of myosin binding protein C, significant data are accumulating, indicating that this protein may act to modulate the primary calcium signals from troponin, and interest in its biological role has grown because of linkages between gene mutations in the cardiac isoform and serious heart disease. © 2011 Wiley Periodicals, Inc. Biopolymers 95: 505–516, 2011.

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Comparative modeling of the three-dimensional structure of the calmodulin-related TCH2 protein from arabidopsis

et al. 1997

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Plants adapt to various stresses by developmental alterations that render them less easily damaged. Expression of the TCH2 gene of Arabidopsis is strongly induced by stimuli such as touch and wind. The gene product, TCH2, belongs to the calmodulin (CaM) family of proteins and contains four highly conserved Ca(2+)-binding EF-hands. We describe here the structure of TCH2 in the fully Ca(2+)-saturated form, constructed using comparative molecular modeling, based on the x-ray structure of paramecium CaM. Like known CaMs, the overall structure consists of two globular domains separated by a linker helix. However, the linker region has added flexibility due to the presence of 5 glycines within a span of 6 residues. In addition, TCH2 is enriched in Lys and Arg residues relative to other CaMs, suggesting a preference for targets which are more negatively charged. Finally, a pair of Cys residues in the C-terminal domain, Cys126 and Cys131, are sufficiently close in space to form a disulfide bridge. These predictions serve to direct future biochemical and structural studies with the overall aim of understanding the role of TCH2 in the cellular response of Arabidopsis to environmental stimuli.

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Refined crystal structure of troponin C from turkey skeletal muscle at 2·0 Å resolution

Cited by 337 publications

References 34 publications

Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy

Solution secondary structure of calcium‐saturated troponin C monomer determined by multidimensional heteronuclear NMR spectroscopy

Invited review: Probing the structures of muscle regulatory proteins using small‐angle solution scattering

Comparative modeling of the three-dimensional structure of the calmodulin-related TCH2 protein from arabidopsis

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