6J72

Crystal structure of IniA from Mycobacterium smegmatis with GTP bound

6J72 の概要

• エントリーDOI: 10.2210/pdb6j72/pdb
• 分子名称: Isoniazid inducible gene protein IniA, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: gtpase, dynamin-like, drug-resistance, hydrolase
• 由来する生物種: Mycolicibacterium smegmatis MC2 155
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67283.11

構造登録者

Wang, M.F.,Guo, X.Y.,Hu, J.J.,Li, J.,Rao, Z.H. (登録日: 2019-01-16, 公開日: 2019-09-11, 最終更新日: 2024-03-27)

主引用文献

Wang, M.,Guo, X.,Yang, X.,Zhang, B.,Ren, J.,Liu, A.,Ran, Y.,Yan, B.,Chen, F.,Guddat, L.W.,Hu, J.,Li, J.,Rao, Z.
Mycobacterial dynamin-like protein IniA mediates membrane fission.
Nat Commun, 10:3906-3906, 2019

PubMed Abstract: Mycobacterium tuberculosis infection remains a major threat to human health worldwide. Drug treatments against tuberculosis (TB) induce expression of several mycobacterial proteins, including IniA, but its structure and function remain poorly understood. Here, we report the structures of Mycobacterium smegmatis IniA in both the nucleotide-free and GTP-bound states. The structures reveal that IniA folds as a bacterial dynamin-like protein (BDLP) with a canonical GTPase domain followed by two helix-bundles (HBs), named Neck and Trunk. The distal end of its Trunk domain exists as a lipid-interacting (LI) loop, which binds to negatively charged lipids for membrane attachment. IniA does not form detectable nucleotide-dependent dimers in solution. However, lipid tethering indicates nucleotide-independent association of IniA on the membrane. IniA also deforms membranes and exhibits GTP-hydrolyzing dependent membrane fission. These results confirm the membrane remodeling activity of BDLP and suggest that IniA mediates TB drug-resistance through fission activity to maintain plasma membrane integrity.

PubMed: 31467269
DOI: 10.1038/s41467-019-11860-z

実験手法

X-RAY DIFFRACTION (2.2 Å)