6ZLO

E2 core of the fungal Pyruvate dehydrogenase complex with asymmetric interior PX30 component

これはPDB形式変換不可エントリーです。

6ZLO の概要

• エントリーDOI: 10.2210/pdb6zlo/pdb
• EMDBエントリー: 11266 11267 11268 11269 11270
• 分子名称: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (1 entity in total)
• 機能のキーワード: acetyl transferase, pyruvate dehydrogenase, protein complex, mitochondria, metabolism, tetrahedral icosahedral, transferase
• 由来する生物種: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
• タンパク質・核酸の鎖数: 60
• 化学式量合計: 1804998.96

構造登録者

Forsberg, B.O.,Howard, R.J.,Aibara, S.,Mortesaei, N.,Lindahl, E. (登録日: 2020-06-30, 公開日: 2020-09-23, 最終更新日: 2024-05-01)

主引用文献

Forsberg, B.O.,Aibara, S.,Howard, R.J.,Mortezaei, N.,Lindahl, E.
Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex.
Nat Commun, 11:4667-4667, 2020

PubMed Abstract: The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) of mammalian PDC, PX selectively recruits E3 to the fungal PDC, but its divergent sequence suggests a distinct structural mechanism. Here, we report reconstructions of PDC from the filamentous fungus Neurospora crassa by cryo-electron microscopy, where we find protein X (PX) interior to the PDC core as opposed to substituting E2 core subunits as in mammals. Steric occlusion limits PX binding, resulting in predominantly tetrahedral symmetry, explaining previous observations in Saccharomyces cerevisiae. The PX-binding site is conserved in (and specific to) fungi, and complements possible C-terminal binding motifs in PX that are absent in mammalian E3BP. Consideration of multiple symmetries thus reveals a differential structural basis for E3BP-like function in fungal PDC.

PubMed: 32938938
DOI: 10.1038/s41467-020-18401-z

実験手法

ELECTRON MICROSCOPY (2.9 Å)