Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
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 transacetyla...
Saved in:
Main Authors: | Jana Škerlová, Jens Berndtsson, Hendrik Nolte, Martin Ott, Pål Stenmark |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2021
|
Subjects: | |
Online Access: | https://doaj.org/article/3ce4dfc9c80943b38a2d9c01e7957c65 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex
by: B. O. Forsberg, et al.
Published: (2020) -
Resveratrol reverses the Warburg effect by targeting the pyruvate dehydrogenase complex in colon cancer cells
by: Elise Saunier, et al.
Published: (2017) -
Arabidopsis phenotyping reveals the importance of alcohol dehydrogenase and pyruvate decarboxylase for aerobic plant growth
by: Irene Ventura, et al.
Published: (2020) -
Astrocytic pyruvate dehydrogenase kinase-2 is involved in hypothalamic inflammation in mouse models of diabetes
by: Md Habibur Rahman, et al.
Published: (2020) -
Hemistepsin A suppresses colorectal cancer growth through inhibiting pyruvate dehydrogenase kinase activity
by: Ling Jin, et al.
Published: (2020)