2V1S

CRYSTAL STRUCTURE OF RAT TOM20-ALDH PRESEQUENCE COMPLEX

「2CUV」から置き換えられました

2V1S の概要

• エントリーDOI: 10.2210/pdb2v1s/pdb
• 関連するPDBエントリー: 1OM2 1WT4 2CUV
• 分子名称: MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20 HOMOLOG, ALDEHYDE DEHYDROGENASE (3 entities in total)
• 機能のキーワード: flavoprotein, mitochondrion, disulfide-bond tethering, steroid biosynthesis, protein transport, sterol biosynthesis, lipid synthesis, transit peptide, phosphorylation, nad, fad, membrane, transport, transmembrane, oxidoreductase, outer membrane, membrane protein/oxidoreductase
• 由来する生物種: RATTUS NORVEGICUS (RAT); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 65910.89

構造登録者

Obita, T.,Igura, M.,Ose, T.,Endo, T.,Maenaka, K.,Kohda, D. (登録日: 2007-05-29, 公開日: 2007-06-12, 最終更新日: 2023-12-13)

主引用文献

Saitoh, T.,Igura, M.,Obita, T.,Ose, T.,Kojima, R.,Maenaka, K.,Endo, T.,Kohda, D.
Tom20 Recognizes Mitochondrial Presequences Through Dynamic Equilibrium Among Multiple Bound States.
Embo J., 26:4777-, 2007

PubMed Abstract: Most mitochondrial proteins are synthesized in the cytosol and imported into mitochondria. The N-terminal presequences of mitochondrial-precursor proteins contain a diverse consensus motif (phi chi chi phi phi, phi is hydrophobic and chi is any amino acid), which is recognized by the Tom20 protein on the mitochondrial surface. To reveal the structural basis of the broad selectivity of Tom20, the Tom20-presequence complex was crystallized. Tethering a presequence peptide to Tom20 through a disulfide bond was essential for crystallization. Unexpectedly, the two crystals with different linker designs provided unique relative orientations of the presequence with respect to Tom20, and neither configuration could fully account for the hydrophobic preference at the three hydrophobic positions of the consensus motif. We propose the existence of a dynamic equilibrium in solution among multiple states including the two bound states. In accordance, NMR 15N relaxation analyses suggested motion on a sub-millisecond timescale at the Tom20-presequence interface. We suggest that the dynamic, multiple-mode interaction is the molecular mechanism facilitating the broadly selective specificity of the Tom20 receptor toward diverse mitochondrial presequences.

PubMed: 17948058
DOI: 10.1038/SJ.EMBOJ.7601888

実験手法

X-RAY DIFFRACTION (2.05 Å)