4P4T

GDP-bound stalkless-MxA

4P4T の概要

• エントリーDOI: 10.2210/pdb4p4t/pdb
• 関連するPDBエントリー: 4P4S 4P4U
• 分子名称: Interferon-induced GTP-binding protein Mx1, GUANOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: gtpase, dynamin-related protein, antiviral, mechano-enzyme, hydrolase, gtp-binding protein, antiviral protein-hydrolase complex, antiviral protein/hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm . Isoform 2: Cytoplasm : P20591
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40760.11

構造登録者

Rennie, M.L.,McKelvie, S.A.,Bulloch, E.M.,Kingston, R.L. (登録日: 2014-03-13, 公開日: 2014-10-22, 最終更新日: 2023-09-27)

主引用文献

Rennie, M.L.,McKelvie, S.A.,Bulloch, E.M.,Kingston, R.L.
Transient Dimerization of Human MxA Promotes GTP Hydrolysis, Resulting in a Mechanical Power Stroke.
Structure, 22:1433-1445, 2014

PubMed Abstract: Myxovirus resistance (Mx) proteins restrict replication of numerous viruses. They are closely related to membrane-remodeling fission GTPases, such as dynamin. Mx proteins can tubulate lipids and form rings or filaments that may interact directly with viral structures. GTPase domain dimerization is thought to allow crosstalk between the rungs of a tubular or helical assembly, facilitating constriction. We demonstrate that the GTPase domain of MxA dimerizes to facilitate catalysis, in a fashion analogous to dynamin. GTP binding is associated with the lever-like movement of structures adjacent to the GTPase domain, while GTP hydrolysis returns MxA to its resting state. Dimerization is not significantly promoted by substrate binding and occurs only transiently, yet is central to catalytic efficiency. Therefore, we suggest dimerization functions to coordinate the activity of spatially adjacent Mx molecules within an assembly, allowing their mechanical power strokes to be synchronized at key points in the contractile cycle.

PubMed: 25295396
DOI: 10.1016/j.str.2014.08.015

実験手法

X-RAY DIFFRACTION (2.3 Å)