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  Crystal structure of the βSer178 -> Pro mutant of tryptophan synthase - A "knock-out" allosteric enzyme

Weyand, M., Schlichting, I., Herde, P., Marabotti, A., & Mozzarelli, A. (2002). Crystal structure of the βSer178 -> Pro mutant of tryptophan synthase - A "knock-out" allosteric enzyme. Journal of Biological Chemistry, 277(12): 1, pp. 10653-10660. Retrieved from http://www.jbc.org/cgi/reprint/277/12/10653.pdf.

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Genre: Zeitschriftenartikel
Alternativer Titel : J. Biol. Chem.

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 Urheber:
Weyand, Michael1, Autor
Schlichting, Ilme2, Autor           
Herde, Petra1, Autor
Marabotti, Anna, Autor
Mozzarelli, Andrea, Autor
Affiliations:
1Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753286              
2Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753289              

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 Zusammenfassung: The catalytic activity of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)/beta(2) complex is allosterically regulated. The hydrogen bond between the helix betaH6 residue betaSer(178) and the loop alphaL6 residue Gly(181) was shown to be critical in ligand-induced inter-subunit signaling, with the alpha-beta communication being completely lost in the mutant betaSer(178) --> Pro (Marabotti, A., De Biase, D., Tramonti, A., Bettati, S., and Mozzarelli, A (2001) J. Biol Chem. 276,17747-17753). The structural basis of the impaired allosteric regulation was investigated by determining the crystal structures of the mutant betaSer(178) --> Pro in the absence and presence of the a-subunit ligands indole-3- acetylglycine and glycerol 3-phosphate. The mutation causes local and distant conformational changes especially in the beta-subunit. The ligand-free structure exhibits larger differences at the N-terminal part of helix betaH6, whereas the enzyme ligand complexes show differences at the C-terminal side. In contrast to the wild-type enzyme loop alphaL6 remains in an open conformation even in the presence of alpha-ligands. This effects the equilibrium between active and inactive conformations of the alpha-active site, altering k(cat) and K- m, and forms the structural basis for the missing allosteric communication between the alpha- and beta-subunits.

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Sprache(n): eng - English
 Datum: 2002-03-22
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 6157
URI: http://www.jbc.org/cgi/reprint/277/12/10653.pdf
 Art des Abschluß: -

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Titel: Journal of Biological Chemistry
  Alternativer Titel : J. Biol. Chem.
Genre der Quelle: Zeitschrift
 Urheber:
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Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 277 (12) Artikelnummer: 1 Start- / Endseite: 10653 - 10660 Identifikator: -