Refined molecular hinge between allosteric and catalytic domain determines allosteric regulation and stability of fungal chorismate mutase
The yeast chorismate mutase is regulated by tyrosine as feedback inhibitor and tryptophan as crosspathway activator. The monomer consists of a catalytic and a regulatory domain covalently linked by the loop L220s (212–226), which functions as a molecular hinge. Two monomers form the active dimeric e...
Uloženo v:
| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2002
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC124454/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11997452/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.092130899 |
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