5GTM

Modified human MxA, nucleotide-free form

5GTM の概要

• エントリーDOI: 10.2210/pdb5gtm/pdb
• 分子名称: Interferon-induced GTP-binding protein Mx1 (2 entities in total)
• 機能のキーワード: hydrolysis, antiviral activity, antiviral protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm . Isoform 2: Cytoplasm : P20591
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 136859.42

構造登録者

Chen, Y.,Gao, S. (登録日: 2016-08-22, 公開日: 2017-05-31, 最終更新日: 2023-11-08)

主引用文献

Chen, Y.,Zhang, L.,Graf, L.,Yu, B.,Liu, Y.,Kochs, G.,Zhao, Y.,Gao, S.
Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET
Nat Commun, 8:15744-15744, 2017

PubMed Abstract: Human myxovirus resistance protein 1 (MxA) restricts a wide range of viruses and is closely related to the membrane-remodelling GTPase dynamin. The functions of MxA rely on domain rearrangements coupled with GTP hydrolysis cycles. To gain insight into this process, we studied real-time domain dynamics of MxA by single-molecule fluorescence resonance energy transfer. We find that the GTPase domain-bundle-signalling-element (BSE) region can adopt either an 'open' or a 'closed' conformation in all nucleotide-loading conditions. Whereas the open conformation is preferred in nucleotide-free, GDP·AlF-bound and GDP-bound forms, loading of GTP activates the relative movement between the two domains and alters the conformational preference to the 'closed' state. Moreover, frequent relative movement was observed between BSE and stalk via hinge 1. On the basis of these results, we suggest how MxA molecules within a helical polymer collectively generate a stable torque through random GTP hydrolysis cycles. Our study provides mechanistic insights into fundamental cellular events such as viral resistance and endocytosis.

PubMed: 28548099
DOI: 10.1038/ncomms15744

実験手法

X-RAY DIFFRACTION (2.896 Å)