Status: Bibliographieeintrag
Standort: ---
Exemplare:
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| Online-Ressource |
Verfasst von: | Feldman-Salit, Anna [VerfasserIn]  |
| Wirtz, Markus [VerfasserIn]  |
| Throm, Christian [VerfasserIn]  |
| Hell, Rüdiger [VerfasserIn]  |
| Wade, Rebecca C. [VerfasserIn]  |
Titel: | Allosterically gated enzyme dynamics in the cysteine synthase complex regulate cysteine biosynthesis in Arabidopsis thaliana |
Verf.angabe: | Anna Feldman-Salit, Markus Wirtz, Esther D. Lenherr, Christian Throm, Michael Hothorn, Klaus Scheffzek, Rüdiger Hell, and Rebecca C. Wade |
E-Jahr: | 2012 |
Jahr: | 8 Februar 2012 |
Umfang: | 11 S. |
Fussnoten: | Gesehen am: 18.05.2017 |
Titel Quelle: | Enthalten in: Structure |
Ort Quelle: | London [u.a.] : Elsevier Science, 1993 |
Jahr Quelle: | 2012 |
Band/Heft Quelle: | 20(2012), 2, Seite 292-302 |
ISSN Quelle: | 1878-4186 |
Abstract: | Summary: Plants and bacteria assimilate sulfur into cysteine. Cysteine biosynthesis involves a bienzyme complex, the cysteine synthase complex (CSC), which consists of serine-acetyl-transferase (SAT) and O-acetyl-serine-(thiol)-lyase (OAS-TL) enzymes. The activity of OAS-TL is reduced by formation of the CSC. Although this reduction is an inherent part of the self-regulation cycle of cysteine biosynthesis, there has until now been no explanation as to how OAS-TL loses activity in plants. Complexation of SAT and OAS-TL involves binding of the C-terminal tail of SAT in one of the active sites of the homodimeric OAS-TL. We here explore the flexibility of the unoccupied active site in Arabidopsis thaliana cytosolic and mitochondrial OAS-TLs. Our results reveal two gates in the OAS-TL active site that define its accessibility. The observed dynamics of the gates show allosteric closure of the unoccupied active site of OAS-TL in the CSC, which can hinder substrate binding, abolishing its turnover to cysteine. |
DOI: | doi:10.1016/j.str.2011.11.019 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Kostenfrei: Volltext ; Verlag: http://dx.doi.org/10.1016/j.str.2011.11.019 |
| Kostenfrei: Volltext: http://www.sciencedirect.com/science/article/pii/S0969212611004655 |
| DOI: https://doi.org/10.1016/j.str.2011.11.019 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1558751688 |
Verknüpfungen: | → Zeitschrift |
Allosterically gated enzyme dynamics in the cysteine synthase complex regulate cysteine biosynthesis in Arabidopsis thaliana / Feldman-Salit, Anna [VerfasserIn]; 8 Februar 2012 (Online-Ressource)
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