Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy.
Abstract: Nuclear magnetic resonance spectra of acylphosphatase were searched for signs of beta-structure, i.e. characteristic nuclear Overhauser enhancement patterns displayed in the two-dimensional spectra, typical chemical shifts, coupling constants and slow 2H-H exchange. The results provided identification of the main-chain resonances of amino acid residues involved in the beta-structure. The full sequential assignment of this region was gained by identification of some amino acid spin systems and their alignment with the primary sequence. The assignment of the side-chains was virtually completed subsequently and a list produced of nuclear magnetic resonance (n.m.r.) constraints derived from the spectra. The beta-structure consists of a beta-sheet with four antiparallel chains, one attached parallel chain, three tight turns and a beta-bulge. The conformation of the beta-sheet was determined by distance geometry calculation using the n.m.r. constraints (174 intraresidual, 107 sequential and 226 long-range distances, 32 torsion angles, phi, and 28 hydrogen bonds) as input. Observation of some interactions between the sheet and previously identified alpha-helical regions made it possible to give an outline of the three-dimensional structure of the enzyme.
Publication Date: 1989-05-20 PubMed ID: 2547076DOI: 10.1016/0022-2836(89)90263-5Google Scholar: Lookup
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Summary
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This research examines the beta-structure in horse muscle acylphosphatase, using nuclear magnetic resonance spectroscopy. The obtained data identified the main-chain resonances of amino acid residues, assigned full sequences, completed side-chain assignments, and outlined the three-dimensional structure of the enzyme.
Identification of Beta-structure
- The researchers used nuclear magnetic resonance spectroscopy to study the acylphosphatase enzyme. They were looking for signs of beta-structure, which are characteristic patterns shown in the two-dimensional spectra, typical chemical shifts, coupling constants, and slow 2H-H exchange.
- The results provided identification of the main-chain resonances of amino acid residues involved in the beta-structure.
Sequential Assignment
- The full sequential assignment of this beta-structure region was achieved by identifying some amino acid spin systems and aligning them with the primary sequence. The assignment of the side-chains was virtually completed afterward.
- A list was produced of NMR constraints derived from the spectra, providing more in-depth information about the structure.
Beta-Structure Composition
- The researchers found that the beta-structure consists of a beta-sheet with four antiparallel chains, one attached parallel chain, three tight turns, and a beta-bulge.
- The conformation of the beta-sheet was determined using distance geometry calculation based on the NMR constraints. These included 174 intraresidual, 107 sequential, and 226 long-range distances, 32 torsion angles, phi, and 28 hydrogen bonds.
Three-Dimensional Structure Outline
- Observations of some interactions between the beta-sheet and previously identified alpha-helical regions enabled the researchers to draw out an initial outline of the three-dimensional structure of the acylphosphatase enzyme.
- This study hence, contributed towards a more comprehensive understanding of the structure of this enzyme, which might have significant implications in its study, modification, and utilization.
Cite This Article
APA
Saudek V, Wormald MR, Williams RJ, Boyd J, Stefani M, Ramponi G.
(1989).
Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy.
J Mol Biol, 207(2), 405-415.
https://doi.org/10.1016/0022-2836(89)90263-5 Publication
Researcher Affiliations
- Inorganic Chemistry Laboratory, University of Oxford, U.K.
MeSH Terms
- Acid Anhydride Hydrolases
- Amino Acid Sequence
- Amino Acids
- Animals
- Horses
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Models, Structural
- Molecular Sequence Data
- Muscles / enzymology
- Phosphoric Monoester Hydrolases
- Protein Conformation
Citations
This article has been cited 6 times.- Jha AK, Freed KF. Solvation effect on conformations of 1,2:dimethoxyethane: charge-dependent nonlinear response in implicit solvent models. J Chem Phys 2008 Jan 21;128(3):034501.
- Modesti A, Taddei N, Chiti F, Bucciantini M, Magherini F, Rigacci S, Stefani M, Raugei G, Ramponi G. Properties of Cys21-mutated muscle acylphosphatases. J Protein Chem 1996 Jan;15(1):27-34.
- Pazzagli L, Cappugi G, Camici G, Manao G, Ramponi G. Bovine testis acylphosphatase: purification and amino acid sequence. J Protein Chem 1993 Oct;12(5):593-601.
- Paoli P, Camici G, Manao G, Ramponi G. 2-Methoxybenzoyl phosphate: a new substrate for continuous fluorimetric and spectrophotometric acyl phosphatase assays. Experientia 1995 Jan 15;51(1):57-62.
- Hoffman DW, Query CC, Golden BL, White SW, Keene JD. RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins. Proc Natl Acad Sci U S A 1991 Mar 15;88(6):2495-9.
- Berti A, Tremori E, Pazzagli L, Degl'Innocenti D, Camici G, Cappugi G, Manao G, Ramponi G. Rat muscle acylphosphatase: purification, amino sequence, and immunological characterization. J Protein Chem 1991 Feb;10(1):91-102.
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