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-Structure paper
タイトル | Cryo-EM structures of mitochondrial ABC transporter ABCB10 in apo and biliverdin-bound form. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 2030, Year 2023 |
掲載日 | 2023年4月11日 |
著者 | Sheng Cao / Yihu Yang / Lili He / Yumo Hang / Xiaodong Yan / Hui Shi / Jiaquan Wu / Zhuqing Ouyang / |
PubMed 要旨 | ABCB10, a member of ABC transporter superfamily that locates in the inner membrane of mitochondria, plays crucial roles in hemoglobin synthesis, antioxidative stress and stabilization of the iron ...ABCB10, a member of ABC transporter superfamily that locates in the inner membrane of mitochondria, plays crucial roles in hemoglobin synthesis, antioxidative stress and stabilization of the iron transporter mitoferrin-1. Recently, it was found that ABCB10 is a mitochondrial biliverdin exporter. However, the molecular mechanism of biliverdin export by ABCB10 remains elusive. Here we report the cryo-EM structures of ABCB10 in apo (ABCB10-apo) and biliverdin-bound form (ABCB10-BV) at 3.67 Å and 2.85 Å resolution, respectively. ABCB10-apo adopts a wide-open conformation and may thus represent the apo form structure. ABCB10-BV forms a closed conformation and biliverdin situates in a hydrophobic pocket in one protomer and bridges the interaction through hydrogen bonds with the opposing one. We also identify cholesterols sandwiched by BVs and discuss the export dynamics based on these structural and biochemical observations. |
リンク | Nat Commun / PubMed:37041204 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.85 - 3.67 Å |
構造データ | EMDB-33603, PDB-7y48: EMDB-33604, PDB-7y49: |
化合物 | ChemComp-CLR: ChemComp-IE5: |
由来 |
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キーワード | MEMBRANE PROTEIN / ABC transporter / biliverdin / ABCB10 |