6H17

Myxococcus xanthus MglA bound to GTPgammaS

6H17 の概要

• エントリーDOI: 10.2210/pdb6h17/pdb
• 分子名称: Mutual gliding-motility protein MglA, MAGNESIUM ION, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: gtpase, motility, cytosolic protein
• 由来する生物種: Myxococcus xanthus DK 1622
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23626.94

構造登録者

Galicia, C.,Cherfils, J. (登録日: 2018-07-11, 公開日: 2019-11-27, 最終更新日: 2024-05-15)

主引用文献

Galicia, C.,Lhospice, S.,Varela, P.F.,Trapani, S.,Zhang, W.,Navaza, J.,Herrou, J.,Mignot, T.,Cherfils, J.
MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus.
Nat Commun, 10:5300-5300, 2019

PubMed Abstract: In Myxococcus xanthus, directed movement is controlled by pole-to-pole oscillations of the small GTPase MglA and its GAP MglB. Direction reversals require that MglA is inactivated by MglB, yet paradoxically MglA and MglB are located at opposite poles at reversal initiation. Here we report the complete MglA/MglB structural cycle combined to GAP kinetics and in vivo motility assays, which uncovers that MglA is a three-state GTPase and suggests a molecular mechanism for concerted MglA/MglB relocalizations. We show that MglA has an atypical GTP-bound state (MglA-GTP*) that is refractory to MglB and is re-sensitized by a feedback mechanism operated by MglA-GDP. By identifying and mutating the pole-binding region of MglB, we then provide evidence that the MglA-GTP* state exists in vivo. These data support a model in which MglA-GDP acts as a soluble messenger to convert polar MglA-GTP* into a diffusible MglA-GTP species that re-localizes to the opposite pole during reversals.

PubMed: 31757955
DOI: 10.1038/s41467-019-13274-3

実験手法

X-RAY DIFFRACTION (1.275 Å)