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
+検索条件
-Structure paper
| タイトル | Plant-specific features of respiratory supercomplex I + III from Vigna radiata. |
|---|---|
| ジャーナル・号・ページ | Nat Plants, Vol. 9, Issue 1, Page 157-168, Year 2023 |
| 掲載日 | 2022年12月29日 |
 著者 | M Maldonado / Z Fan / K M Abe / J A Letts /  |
| PubMed 要旨 | The last steps of cellular respiration-an essential metabolic process in plants-are carried out by mitochondrial oxidative phosphorylation. This process involves a chain of multi-subunit membrane ...The last steps of cellular respiration-an essential metabolic process in plants-are carried out by mitochondrial oxidative phosphorylation. This process involves a chain of multi-subunit membrane protein complexes (complexes I-V) that form higher-order assemblies called supercomplexes. Although supercomplexes are the most physiologically relevant form of the oxidative phosphorylation complexes, their functions and structures remain mostly unknown. Here we present the cryogenic electron microscopy structure of the supercomplex I + III from Vigna radiata (mung bean). The structure contains the full subunit complement of complex I, including a newly assigned, plant-specific subunit. It also shows differences in the mitochondrial processing peptidase domain of complex III relative to a previously determined supercomplex with complex IV. The supercomplex interface, while reminiscent of that in other organisms, is plant specific, with a major interface involving complex III's mitochondrial processing peptidase domain and no participation of complex I's bridge domain. The complex I structure suggests that the bridge domain sets the angle between the enzyme's two arms, limiting large-scale conformational changes. Moreover, complex I's catalytic loops and its response in active-to-deactive assays suggest that, in V. radiata, the resting complex adopts a non-canonical state and can sample deactive- or open-like conformations even in the presence of substrate. This study widens our understanding of the possible conformations and behaviour of complex I and supercomplex I + III. Further studies of complex I and its supercomplexes in diverse organisms are needed to determine the universal and clade-specific mechanisms of respiration. |
 リンク | Nat Plants / PubMed:36581760 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.2 - 5.4 Å |
| 構造データ | EMDB-27934, PDB-8e73:  EMDB-28798: Vigna radiata supercomplex I+III2 - bridgeless classes 1  EMDB-28799: Vigna radiata respiratory complex I  EMDB-29088: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex I bridge  EMDB-29089: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex I heel  EMDB-29090: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex I Pd domain  EMDB-29091: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex III2 dimer  EMDB-29092: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex I N module  EMDB-29093: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex III2 proximal MPP domain  EMDB-29094: Focused refinement of V. radiata respiratory supercomplex I+III2 around complex III2 distal MPP domain  EMDB-29095: V. radiata respiratory supercomplex I+III2 bridged class 2  EMDB-29190: V. radiata respiratory supercomplex I+III2 bridgeless class 3  EMDB-29191: V. radiata respiratory supercomplex I+III2 bridgeless class 2  EMDB-29203: V. radiata respiratory supercomplex I+III2 bridgeless class 4 |
| 化合物 |  ChemComp-PC1:  ChemComp-CDL:  ChemComp-HEM:  ChemComp-3PE:  ChemComp-HEC:  ChemComp-NDP:  ChemComp-ZMP:  ChemComp-FE:  ChemComp-ZN:  ChemComp-SF4:  ChemComp-FES:  ChemComp-FMN: |
| 由来 |
|
 キーワード | ELECTRON TRANSPORT / respiratory supercomplex / nadh-cyt c oxidoreductase / membrane complex |
vigna radiata (リョクトウ)