6KYL

Crystal Structure of Phosphatidic acid Transporter Ups1/Mdm35 in Complex with (2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoate

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6KYL の概要

• エントリーDOI: 10.2210/pdb6kyl/pdb
• 分子名称: Mitochondrial distribution and morphology protein 35, Protein UPS1, mitochondrial, (2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoate (3 entities in total)
• 機能のキーワード: lipid transport, transport protein
• 由来する生物種: Saccharomyces cerevisiae S288c (Yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63695.97

構造登録者

Lu, J.,Chan, K.C.,Zhai, Y.,Fan, J.,Sun, F. (登録日: 2019-09-19, 公開日: 2019-10-02, 最終更新日: 2024-10-23)

主引用文献

Lu, J.,Chan, C.,Yu, L.,Fan, J.,Sun, F.,Zhai, Y.
Molecular mechanism of mitochondrial phosphatidate transfer by Ups1.
Commun Biol, 3:468-468, 2020

PubMed Abstract: Cardiolipin, an essential mitochondrial physiological regulator, is synthesized from phosphatidic acid (PA) in the inner mitochondrial membrane (IMM). PA is synthesized in the endoplasmic reticulum and transferred to the IMM via the outer mitochondrial membrane (OMM) under mediation by the Ups1/Mdm35 protein family. Despite the availability of numerous crystal structures, the detailed mechanism underlying PA transfer between mitochondrial membranes remains unclear. Here, a model of Ups1/Mdm35-membrane interaction is established using combined crystallographic data, all-atom molecular dynamics simulations, extensive structural comparisons, and biophysical assays. The α2-loop, L2-loop, and α3 helix of Ups1 mediate membrane interactions. Moreover, non-complexed Ups1 on membranes is found to be a key transition state for PA transfer. The membrane-bound non-complexed Ups1/ membrane-bound Ups1 ratio, which can be regulated by environmental pH, is inversely correlated with the PA transfer activity of Ups1/Mdm35. These results demonstrate a new model of the fine conformational changes of Ups1/Mdm35 during PA transfer.

PubMed: 32843686
DOI: 10.1038/s42003-020-01121-x

実験手法

X-RAY DIFFRACTION (3.55 Å)