+検索条件
-Structure paper
| タイトル | Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase in . |
|---|---|
| ジャーナル・号・ページ | bioRxiv, Year 2025 |
| 掲載日 | 2025年12月23日 |
著者 | Radha P Somarathne / Riti Shrestha / Mishghan Zehra / Cole Brodeur / David Bhella / Wing-Cheung Lai / Amit Meir / Clarissa L Durie / ![]() |
| PubMed 要旨 | 3-Methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent carboxylase that metabolizes the amino acid leucine. MCC is present in bacteria, fungi, plants, and animals. In humans, its overexpression ...3-Methylcrotonyl-CoA carboxylase (MCC) is a biotin-dependent carboxylase that metabolizes the amino acid leucine. MCC is present in bacteria, fungi, plants, and animals. In humans, its overexpression is linked to cancer, and its deficiency is linked to inborn errors of metabolism with severe consequences, so understanding its structure and function has far reaching implications. Here, we explore the MCC from , a pathogenic bacterium with a biphasic life cycle. Our endogenous holoenzyme yielded the highest resolution cryo-EM structure of MCC to date, allowing for identification of protein components by the machine learning tool ModelAngelo, confirmed independently by mass spectrometry. We also observed, for the first time, enhanced filamentation of MCC upon substrate binding. We propose that this filamentation, previously observed in the eukaryotes, but not in bacteria, may be important for cellular processes such as differentiation of life cycle or cell division. |
リンク | bioRxiv / PubMed:41509382 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.48 - 2.68 Å |
| 構造データ | EMDB-56131, PDB-9tqc: EMDB-56149, PDB-9tqg: |
| 化合物 | ![]() ChemComp-BTI: |
| 由来 |
|
キーワード | LIGASE / 3-methylcrotonyl-CoA carboxylase / biotin |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク





キーワード