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-Structure paper
タイトル | 3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme. |
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ジャーナル・号・ページ | Commun Biol, Vol. 4, Issue 1, Page 684, Year 2021 |
掲載日 | 2021年6月3日 |
著者 | Melisa Lázaro / Roberto Melero / Charlotte Huet / Jorge P López-Alonso / Sandra Delgado / Alexandra Dodu / Eduardo M Bruch / Luciano A Abriata / Pedro M Alzari / Mikel Valle / María-Natalia Lisa / |
PubMed 要旨 | Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs) contain long N- ...Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs in bacterial physiology, the lack of structural data for these enzymes has limited the progress of functional studies. Here we show that the mycobacterial L-GDH (mL-GDH) adopts a quaternary structure that is radically different from that of related low molecular weight enzymes. Intersubunit contacts in mL-GDH involve a C-terminal domain that we propose as a new fold and a flexible N-terminal segment comprising ACT-like and PAS-type domains that could act as metabolic sensors for allosteric regulation. These findings uncover unique aspects of the structure-function relationship in the subfamily of L-GDHs. |
リンク | Commun Biol / PubMed:34083757 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 3.59 - 6.6 Å |
構造データ | EMDB-11606, PDB-7a1d: EMDB-11612: EMDB-11613: PDB-7jsr: |
由来 |
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キーワード | OXIDOREDUCTASE / large glutamate dehydrogenase Mycobacterium metabolism / large glutamate dehydrogenase / Mycobacterium / metabolism |