Related ArticlesRemarkable Rigidity of the Single ?-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.
J Am Chem Soc. 2019 06 05;141(22):9004-9017
Authors: Barnes CA, Shen Y, Ying J, Takagi Y, Torchia DA, Sellers JR, Bax A
Abstract
Although the ?-helix has long been recognized as an all-important element of secondary structure, it generally requires stabilization by tertiary interactions with other parts of a protein's structure. Highly charged single ?-helical (SAH) domains, consisting of a high percentage (>75%) of Arg, Lys, and Glu residues, are exceptions to this rule but have been difficult to characterize structurally. Our study focuses on the 68-residue medial tail domain of myosin-VI, which is found to contain a highly ordered ?-helical structure extending from Glu-6 to Lys-63. High hydrogen exchange protection factors (15-150), small (ca. 4 Hz) 3 JHNH? couplings, and a near-perfect fit to an ideal model ?-helix for its residual dipolar couplings (RDCs), measured in a filamentous phage medium, support the high regularity of this helix. Remarkably, the hydrogen exchange rates are far more homogeneous than the protection factors derived from them, suggesting that for these transiently broken helices the intrinsic exchange rates derived from the amino acid sequence are not appropriate reference values. 15N relaxation data indicate a very high degree of rotational diffusion anisotropy ( D?/ D? ? 7.6), consistent with the hydrodynamic behavior predicted for such a long, nearly straight ?-helix. Alignment of the helix by a paramagnetic lanthanide ion attached to its N-terminal region shows a decrease in alignment as the distance from the tagging site increases. This decrease yields a precise measure for the persistence length of 224 ± 10 Å at 20 °C, supporting the idea that the role of the SAH helix is to act as an extension of the myosin-VI lever arm.
[NMR paper] Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Intrinsic differences in backbone dynamics between wild type and DNA-contact mutants of p53 DNA binding domain revealed by NMR spectroscopy.
Biochemistry. 2017 Aug 24;:
Authors: Rasquinha JA, Bej A, Dutta S, Mukherjee S
Abstract
Mutations in p53's DNA binding domain (p53DBD) are associated with 50% of all cancers, making it an essential system to investigate in order to understand the...
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[NMR paper] ?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
Proc Natl Acad Sci U S A. 2014 Dec 30;
Authors: Vasa S, Lin L, Shi C, Habenstein B, Riedel D, Kühn J, Thanbichler M, Lange A
Abstract
Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central...
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01-01-2015 11:00 PM
[NMR paper] NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase.
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Related Articles NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase.
Protein Pept Lett. 2014 Mar 28;
Authors: Sharma AK, Rigby AC
Abstract
Protein-protein interactions between the C-terminal domain of Myosin Binding Subunit (MBS) of MLC Phosphatase (MBSCT180; C-terminal 180 aa) and the N-terminal coiled coil (CC) leucine zipper (LZ)...
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[NMR paper] A General Method for Constructing Atomic-Resolution RNA Ensembles using NMR Residual Dipolar Couplings: The Basis for Inter-helical Motions Revealed.
A General Method for Constructing Atomic-Resolution RNA Ensembles using NMR Residual Dipolar Couplings: The Basis for Inter-helical Motions Revealed.
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J Am Chem Soc. 2013 Mar 8;
Authors: Salmon L, Bascom GD, Andricioaei I, Al-Hashimi HM
Abstract
The ability to modulate alignment and measure multiple independent sets of NMR residual dipolar couplings (RDCs) has made it possible...
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03-12-2013 07:09 PM
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
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Biochem Biophys Res Commun. 2011 Apr 19;
Authors: Lee DH, Ha JH, Kim Y, Bae KH, Park JY, Choi WS, Yoon HS, Park SG, Park BC, Yi GS, Chi SW
Clusterin (CLU) is a multifunctional glycoprotein that is overexpressed in prostate and breast cancers. Although CLU is known to be involved in the regulation...
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04-30-2011 12:36 PM
[NMR paper] Validation of helical tilt angles in the solution NMR structure of the Z domain of St
Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data.
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Protein Sci. 2004 Feb;13(2):549-54
Authors: Zheng D, Aramini JM, Montelione GT
Staphylococcal protein A (SpA) is a virulence factor from Staphylococcus aureus that is able to bind to...
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[NMR paper] Structure determination of a peptide model of the repeated helical domain in Samia cy
Structure determination of a peptide model of the repeated helical domain in Samia cynthia ricini silk fibroin before spinning by a combination of advanced solid-state NMR methods.
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J Am Chem Soc. 2003 Jun 18;125(24):7230-7
Authors: Nakazawa Y, Asakura T
Fibrous proteins unlike globular proteins, contain repetitive amino acid sequences, giving rise...
Remarkable Rigidity of the Single ?-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.
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