2G3K
Crystal structure of the C-terminal domain of Vps28
2G3K の概要
エントリーDOI | 10.2210/pdb2g3k/pdb |
分子名称 | Vacuolar protein sorting-associated protein VPS28 (2 entities in total) |
機能のキーワード | 4 helix bundle, transport protein |
由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
細胞内の位置 | Cytoplasm: Q02767 |
タンパク質・核酸の鎖数 | 7 |
化学式量合計 | 76667.03 |
構造登録者 | Pineda-Molina, E.,Belrhali, H.,Piefer, A.J.,Akula, I.,Bates, P.,Weissenhorn, W. (登録日: 2006-02-20, 公開日: 2006-06-27, 最終更新日: 2024-10-30) |
主引用文献 | Pineda-Molina, E.,Belrhali, H.,Piefer, A.J.,Akula, I.,Bates, P.,Weissenhorn, W. The crystal structure of the C-terminal domain of Vps28 reveals a conserved surface required for Vps20 recruitment. Traffic, 7:1007-1016, 2006 Cited by PubMed Abstract: The endosomal sorting complex I required for transport (ESCRT-I) is composed of the three subunits Vps23/Tsg101, Vps28 and Vps37. ESCRT-I is recruited to cellular membranes during multivesicular endosome biogenesis and by enveloped viruses such as HIV-1 to mediate budding from the cell. Here, we describe the crystal structure of a conserved C-terminal domain from Sacharomyces cerevisiae Vps28 (Vps28-CTD) at 3.05 A resolution which folds independently into a four-helical bundle structure. Co-expression experiments of Vps28-CTD, Vps23 and Vps37 suggest that Vps28-CTD does not directly participate in ESCRT-I assembly and may thus act as an adaptor module for downstream interaction partners. We show through mutagenesis studies that Vps28-CTD employs its strictly conserved surface in the interaction with the ESCRT-III factor Vps20. Furthermore, we present evidence that Vps28-CTD is sufficient to rescue an equine infectious anaemia virus (EIAV) Gag late domain deletion. Vps28-CTD mutations abolishing Vps20 interaction in vitro also prevent the rescue of the EIAV Gag late domain mutant consistent with a potential direct Vps28-ESCRT-III Vps20 recruitment. Therefore, the physiological relevant EIAV Gag-Alix interaction can be functionally replaced by a Gag-Vps28-CTD fusion. Because both Alix and Vps28-CTD can directly recruit ESCRT-III proteins, ESCRT-III assembly coupled to Vps4 action may therefore constitute the minimal budding machinery for EIAV release. PubMed: 16749904DOI: 10.1111/j.1600-0854.2006.00440.x 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.05 Å) |
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