Transferred Nuclear Overhauser Effect Study of the C-Terminal Helix of Yeast Phosphoglycerate Kinase: NMR Solution Structure of the C-Terminal Bound Peptide
Two-dimensional 1H nuclear magnetic resonance spectroscopy is used to determine the structure of the C-terminal complementary peptide (404-415) bound to a mutant phosphoglycerate kinase (1-403). Conformational changes in the peptide induced by the formation of the peptide-protein complex are followe...
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Veröffentlicht in: | Biochemistry (Easton) 1995, Vol.34 (3), p.842-846 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Two-dimensional 1H nuclear magnetic resonance spectroscopy is used to determine the structure of the C-terminal complementary peptide (404-415) bound to a mutant phosphoglycerate kinase (1-403). Conformational changes in the peptide induced by the formation of the peptide-protein complex are followed by transferred nuclear Overhauser effect spectroscopy. Measurement of transferred NOEs and molecular modeling reveal an alpha-helix fold in the 405-409 region. This fold is in good agreement with the corresponding helix XIV of the crystallographic structure of wild-type PGK (Watson et al., 1982). The role of the alpha-helix from the C-terminal peptide in the recovery of catalytic activity in the mutant PGK is discussed |
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ISSN: | 0006-2960 1520-4995 |
DOI: | 10.1021/bi00003a018 |