3TOW

Crystal Structure of the MABP Domain of MVB12B of Human ESCRT-I Complex

3TOW の概要

• エントリーDOI: 10.2210/pdb3tow/pdb
• 分子名称: Multivesicular body subunit 12B (2 entities in total)
• 機能のキーワード: beta prism, membrane binding domain, negatively charged membrane, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endosome (Probable): Q9H7P6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17227.84

構造登録者

Boura, E.,Hurley, J.H. (登録日: 2011-09-06, 公開日: 2012-01-11, 最終更新日: 2024-02-28)

主引用文献

Boura, E.,Hurley, J.H.
Structural basis for membrane targeting by the MVB12-associated beta-prism domain of the human ESCRT-I MVB12 subunit.
Proc.Natl.Acad.Sci.USA, 109:1901-1906, 2012

PubMed Abstract: MVB12-associated β-prism (MABP) domains are predicted to occur in a diverse set of membrane-associated bacterial and eukaryotic proteins, but their existence, structure, and biochemical properties have not been characterized experimentally. Here, we find that the MABP domains of the MVB12A and B subunits of ESCRT-I are functional modules that bind in vitro to liposomes containing acidic lipids depending on negative charge density. The MABP domain is capable of autonomously localizing to subcellular puncta and to the plasma membrane. The 1.3-Å atomic resolution crystal structure of the MVB12B MABP domain reveals a β-prism fold, a hydrophobic membrane-anchoring loop, and an electropositive phosphoinositide-binding patch. The basic patch is open, which explains how it senses negative charge density but lacks stereoselectivity. These observations show how ESCRT-I could act as a coincidence detector for acidic phospholipids and protein ligands, enabling it to function both in protein transport at endosomes and in cytokinesis and viral budding at the plasma membrane.

PubMed: 22232651
DOI: 10.1073/pnas.1117597109

実験手法

X-RAY DIFFRACTION (1.34 Å)