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PMID: 8075538 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin.

Journal of biomolecular NMR ·Vol. 4 ·No. 4 ·1994-07-00 ·Pages 491-504

Thériault Y, Pochapsky TC, Dalvit C, Chiu ML, Sligar SG, Wright PE

Abstract

Sequence-specific backbone 1H and 15N resonance assignments have been made for 95% of the amino acids in sperm whale myoglobin, complexed with carbon monoxide (MbCO). Many assignments for side-chain resonances have also been obtained. Assignments were made by analysis of an extensive series of homonuclear 2D spectra, measured with unlabeled protein, and both 2D and 3D 1H-15N-correlated spectra obtained from uniformly 15N-labeled myoglobin. Patterns of medium-range NOE connectivities indicate the presence of eight helices in positions that are very similar to those found in the crystal structures of sperm whale myoglobin. The resonance assignments of MbCO form the basis for determination of the solution structure and for hydrogen-exchange measurements to probe the stability and folding pathways of myoglobin. They will also form a basis for assignment of the spectra of single-site mutants with altered ligand-binding properties.

MeSH Terms
Amino Acid Sequence Animals Carbon Monoxide/chemistry Hydrogen Magnetic Resonance Spectroscopy Molecular Sequence Data Myoglobin/chemistry Nitrogen Isotopes Protein Structure, Secondary Recombinant Fusion Proteins/chemistry Whales/blood
Chemicals
Myoglobin Nitrogen Isotopes Recombinant Fusion Proteins carboxymyoglobin Carbon Monoxide Hydrogen
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Thériault Y
Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.
Pochapsky T C
Dalvit C
Chiu M L
Sligar S G
Wright P E
References (38)
38 references, click to expand
  1. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale.
    J Mol Biol. 1977 Mar 5;110(3):569-84 PMID: 845960
  2. Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale.
    J Mol Biol. 1977 Mar 5;110(3):537-68 PMID: 845959
  3. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin.
    Nature. 1981 Jul 2;292(5818):81-2 PMID: 7278969
  4. A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate.
    J Biol Chem. 1992 Jul 15;267(20):14443-50 PMID: 1629229
  5. The mechanism of autooxidation of myoglobin.
    J Biol Chem. 1993 Apr 5;268(10):6995-7010 PMID: 8463233
  6. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules.
    Biochem Biophys Res Commun. 1980 Jul 16;95(1):1-6 PMID: 7417242
  7. Electrostatic interactions in wild-type and mutant recombinant human myoglobins.
    Biochemistry. 1989 May 2;28(9):3771-81 PMID: 2751994
  8. Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin.
    Biochim Biophys Acta. 1985 Nov 29;832(2):175-85 PMID: 4063376
  9. Ligand and proton exchange dynamics in recombinant human myoglobin mutants.
    J Mol Biol. 1989 May 5;207(1):289-99 PMID: 2544737
  10. Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin.
    J Mol Biol. 1981 Nov 25;153(1):117-46 PMID: 7338909
  11. Comparison of the dynamics of myoglobin in different crystal forms.
    Biophys J. 1990 Feb;57(2):381-3 PMID: 2180490
  12. Complete assignment of the 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Application of an integrated approach to spin system identification in proteins.
    J Mol Biol. 1988 Aug 5;202(3):603-22 PMID: 3172229
  13. Heteronuclear three-dimensional NMR spectroscopy of isotopically labelled biological macromolecules.
    Q Rev Biophys. 1990 May;23(2):97-131 PMID: 2188281
  14. Expression in Escherichia coli of a synthetic gene coding for horse heart myoglobin.
    Protein Eng. 1991 Jun;4(5):585-92 PMID: 1891466
  15. Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants.
    J Biol Chem. 1992 Nov 5;267(31):22022-34 PMID: 1429552
  16. CO recombination to human myoglobin mutants in glycerol-water solutions.
    Biochemistry. 1993 Mar 9;32(9):2202-12 PMID: 8443162
  17. Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: application to interleukin 1 beta.
    Biochemistry. 1989 Jul 25;28(15):6150-6 PMID: 2675964
  18. Molecular dynamics simulations of heme reorientational motions in myoglobin.
    Biophys J. 1993 Mar;64(3):869-85 PMID: 8471731
  19. Multiple conformational states of proteins: a molecular dynamics analysis of myoglobin.
    Science. 1987 Jan 16;235(4786):318-21 PMID: 3798113
  20. Crystal structure of myoglobin from a synthetic gene.
    Proteins. 1990;7(4):358-65 PMID: 2199973
  21. Assignment of resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of sperm whale myoglobin by phase-sensitive two-dimensional techniques.
    J Mol Biol. 1987 Mar 20;194(2):313-27 PMID: 3612809
  22. Apomyoglobin as a molecular recognition surface: expression, reconstitution and crystallization of recombinant porcine myoglobin in Escherichia coli.
    Protein Eng. 1988 Sep;2(3):233-7 PMID: 3070546
  23. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins.
    Biochem Biophys Res Commun. 1983 Jun 29;113(3):967-74 PMID: 6307308
  24. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics.
    Nature. 1979 Aug 16;280(5723):558-63 PMID: 460437
  25. Cloning, expression in Escherichia coli, and reconstitution of human myoglobin.
    Proc Natl Acad Sci U S A. 1985 Sep;82(17):5681-4 PMID: 3898068
  26. High-level expression of sperm whale myoglobin in Escherichia coli.
    Proc Natl Acad Sci U S A. 1987 Dec;84(24):8961-5 PMID: 3321062
  27. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin.
    Science. 1993 Nov 5;262(5135):892-6 PMID: 8235610
  28. Structure and refinement of oxymyoglobin at 1.6 A resolution.
    J Mol Biol. 1980 Oct 5;142(4):531-54 PMID: 7463482
  29. Ligand binding to synthetic mutant myoglobin (His-E7----Gly): role of the distal histidine.
    Proc Natl Acad Sci U S A. 1988 Nov;85(22):8497-501 PMID: 3186740
  30. Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
    Biochemistry. 1990 Apr 10;29(14):3542-56 PMID: 2354151
  31. Multiple-quantum nuclear magnetic resonance.
    Methods Enzymol. 1989;176:114-34 PMID: 2811682
  32. Molecular dynamics of myoglobin at 298 degrees K. Results from a 300-ps computer simulation.
    Biophys J. 1985 Sep;48(3):509-18 PMID: 3840041
  33. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.
    J Mol Biol. 1982 Mar 5;155(3):321-46 PMID: 7077676
  34. Dynamics of ligand binding to heme proteins.
    J Mol Biol. 1979 Aug 15;132(3):343-68 PMID: 533895
  35. A neutron diffraction analysis of myoglobin. 3. Hydrogen-deuterium bonding in side chains.
    Cold Spring Harb Symp Quant Biol. 1972;36:569-75 PMID: 4508169
  36. Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering.
    Biochem Biophys Res Commun. 1983 Dec 16;117(2):479-85 PMID: 6661238
  37. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution.
    J Mol Biol. 1986 Nov 5;192(1):133-54 PMID: 3820301
  38. Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K.
    Proc Natl Acad Sci U S A. 1982 Aug;79(16):4967-71 PMID: 6956905
Article Info
Journal
Journal of biomolecular NMR
Abbr.
J Biomol NMR
ISSN
0925-2738
Published
1994-07-00
Pages
491-504
Language
English
Region
Netherlands
NLM ID
9110829
Subset
IM
Grants
NIDDK NIH HHS · DK34909 · United States
NIGMS NIH HHS · GM31756 · United States
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