NMR structure of the sterol carrier protein-2

Implications for the biological role

Francisco López García, Thomas Szyperski, Jim Dyer, Thomas Choinowski, Udo Seedorf, Helmut Hauser, Kurt Wüthrich

Research output: Contribution to journalArticleResearchpeer-review

48 Citations (Scopus)

Abstract

The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone 15N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for Investigations of the mode of action of SCP2. The SCP2 fold is formed by a five-stranded β-sheet and four α-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the β-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spinlabeled substrate 16-doxylstearic acid. In the free protein, the lipid-binding site is covered by the C-terminal segment 105-123, suggesting that this polypeptide segment, which carries the peroxisomal targeting signal (PTS1), might be involved in the regulation of ligand binding. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)595-603
Number of pages9
JournalJournal of Molecular Biology
Volume295
Issue number3
DOIs
StatePublished - 21 Jan 2000

Fingerprint

Peptides
Fatty Acids
Binding Sites
Ligands
Lipids
Amino Acids
sterol carrier proteins
Proteins
16-nitroxystearic acid

Keywords

  • NMR
  • Nitroxide spin labels
  • Protein dynamics
  • Protein structure
  • Sterol carrier protein 2

Cite this

García, F. L., Szyperski, T., Dyer, J., Choinowski, T., Seedorf, U., Hauser, H., & Wüthrich, K. (2000). NMR structure of the sterol carrier protein-2: Implications for the biological role. Journal of Molecular Biology, 295(3), 595-603. https://doi.org/10.1006/jmbi.1999.3355
García, Francisco López ; Szyperski, Thomas ; Dyer, Jim ; Choinowski, Thomas ; Seedorf, Udo ; Hauser, Helmut ; Wüthrich, Kurt. / NMR structure of the sterol carrier protein-2 : Implications for the biological role. In: Journal of Molecular Biology. 2000 ; Vol. 295, No. 3. pp. 595-603.
@article{b1667486d28a466983946db7ea70327d,
title = "NMR structure of the sterol carrier protein-2: Implications for the biological role",
abstract = "The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone 15N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for Investigations of the mode of action of SCP2. The SCP2 fold is formed by a five-stranded β-sheet and four α-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the β-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spinlabeled substrate 16-doxylstearic acid. In the free protein, the lipid-binding site is covered by the C-terminal segment 105-123, suggesting that this polypeptide segment, which carries the peroxisomal targeting signal (PTS1), might be involved in the regulation of ligand binding. (C) 2000 Academic Press.",
keywords = "NMR, Nitroxide spin labels, Protein dynamics, Protein structure, Sterol carrier protein 2",
author = "Garc{\'i}a, {Francisco L{\'o}pez} and Thomas Szyperski and Jim Dyer and Thomas Choinowski and Udo Seedorf and Helmut Hauser and Kurt W{\"u}thrich",
year = "2000",
month = "1",
day = "21",
doi = "10.1006/jmbi.1999.3355",
language = "English",
volume = "295",
pages = "595--603",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

García, FL, Szyperski, T, Dyer, J, Choinowski, T, Seedorf, U, Hauser, H & Wüthrich, K 2000, 'NMR structure of the sterol carrier protein-2: Implications for the biological role', Journal of Molecular Biology, vol. 295, no. 3, pp. 595-603. https://doi.org/10.1006/jmbi.1999.3355

NMR structure of the sterol carrier protein-2 : Implications for the biological role. / García, Francisco López; Szyperski, Thomas; Dyer, Jim; Choinowski, Thomas; Seedorf, Udo; Hauser, Helmut; Wüthrich, Kurt.

In: Journal of Molecular Biology, Vol. 295, No. 3, 21.01.2000, p. 595-603.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - NMR structure of the sterol carrier protein-2

T2 - Implications for the biological role

AU - García, Francisco López

AU - Szyperski, Thomas

AU - Dyer, Jim

AU - Choinowski, Thomas

AU - Seedorf, Udo

AU - Hauser, Helmut

AU - Wüthrich, Kurt

PY - 2000/1/21

Y1 - 2000/1/21

N2 - The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone 15N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for Investigations of the mode of action of SCP2. The SCP2 fold is formed by a five-stranded β-sheet and four α-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the β-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spinlabeled substrate 16-doxylstearic acid. In the free protein, the lipid-binding site is covered by the C-terminal segment 105-123, suggesting that this polypeptide segment, which carries the peroxisomal targeting signal (PTS1), might be involved in the regulation of ligand binding. (C) 2000 Academic Press.

AB - The determination of the NMR structure of the sterol carrier protein-2 (SCP2), analysis of backbone 15N spin relaxation parameters and NMR studies of nitroxide spin-labeled substrate binding are presented as a new basis for Investigations of the mode of action of SCP2. The SCP2 fold is formed by a five-stranded β-sheet and four α-helices. Fatty acid binding to a hydrophobic surface area formed by amino acid residues of the first and third helices, and the β-sheet, which are all located in the polypeptide segment 8-102, was identified with the use of the spinlabeled substrate 16-doxylstearic acid. In the free protein, the lipid-binding site is covered by the C-terminal segment 105-123, suggesting that this polypeptide segment, which carries the peroxisomal targeting signal (PTS1), might be involved in the regulation of ligand binding. (C) 2000 Academic Press.

KW - NMR

KW - Nitroxide spin labels

KW - Protein dynamics

KW - Protein structure

KW - Sterol carrier protein 2

UR - http://www.scopus.com/inward/record.url?scp=0034695426&partnerID=8YFLogxK

U2 - 10.1006/jmbi.1999.3355

DO - 10.1006/jmbi.1999.3355

M3 - Article

VL - 295

SP - 595

EP - 603

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -