| Autor: |
Jana Škerlová, Jens Berndtsson, Hendrik Nolte, Martin Ott, Pål Stenmark |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
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| Zdroj: |
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2041-1723 |
| DOI: |
10.1038/s41467-021-25570-y |
| Popis: |
The pyruvate dehydrogenase complex (PDHc) is a large multienzyme complex that converts pyruvate into acetyl-coenzyme A and in E. coli the core of the PDHc is formed by 24 copies of dihydrolipoyl transacetylase. Here, the authors present the cryo-EM structure of the E. coli dihydrolipoyl transacetylase 24-mer core in a native resting state including lipoyl domains, and discuss the mechanism of substrate shuttling by the lipoyl domains. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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