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-Structure paper
| タイトル | Structural insights into metallocluster trafficking in the nitrogenase assembly scaffold NifEN. |
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| ジャーナル・号・ページ | Nat Catal, Vol. 9, Issue 3, Page 281-294, Year 2026 |
| 掲載日 | 2026年3月3日 |
著者 | Bryan Neumann / Kristal A Brandon / Robert Quechol / Diana S Suder / Chi Chung Lee / Yimo Yang / Kamil Górecki / Jared A Wiig / Yilin Hu / Shane Gonen / Markus W Ribbe / ![]() |
| PubMed 要旨 | Nitrogenase catalyses small-molecule activation, and has great relevance to agronomy, environment and energy. Understanding the assembly of the complex nitrogenase cofactor is a decades-long goal in ...Nitrogenase catalyses small-molecule activation, and has great relevance to agronomy, environment and energy. Understanding the assembly of the complex nitrogenase cofactor is a decades-long goal in the field, and structural insights into this process remain scarce. Here we report a cryogenic electron microscopy (cryo-EM) study of heterologously expressed NifEN, a key player converting the precursor (L-cluster) to a mature cofactor (M-cluster). Structural analyses of apo- and holo-NifEN demonstrate major conformational changes triggered by L-cluster incorporation. Further examinations of NifEN structures with inwardly and outwardly bound L-clusters, coupled with supporting mutational studies, AlphaFold 3 predictions and negative-stain EM analyses of NifEN complexed with upstream (NifB) and downstream (NifH) assembly partners, reveal a tunnel linking NifEN with NifB and NifH, with NifEN serving as a dynamic hub that coordinates L-cluster reception, maturation and delivery via conformation-gated metallocluster trafficking. |
リンク | Nat Catal / PubMed:41908675 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 14.8 - 19.0 Å |
| 構造データ | ![]() EMDB-73406: Negative stained A. vinelandii NifEN-B' fusion ![]() EMDB-73407: Negative stained A. vinelandii NifEN/NifH ADPxAIF4- stabilized complex |
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Azotobacter vinelandii DJ (窒素固定)