7Z3C

Solution structure of GltJ GYF domain from Myxococcus xanthus

Summary for 7Z3C

• Entry DOI: 10.2210/pdb7z3c/pdb
• NMR Information: BMRB: 51096
• Descriptor: Adventurous gliding motility protein X (1 entity in total)
• Functional Keywords: protein, motility, gyf domain, myxococcus xanthus, adventurous motility, gliding, focal adhesion complex, adhesion, regulatory domain, myxobacteria, cell adhesion
• Biological source: Myxococcus xanthus
• Total number of polymer chains: 1
• Total formula weight: 9329.45

Authors

Attia, B.,My, L.,Castaing, J.P.,Le Guenno, H.,Espinosa, L.,Schmidt, V.,Nouailler, M.,Bornet, O.,Elantak, L.,Mignot, T. (deposition date: 2022-03-02, release date: 2023-02-22, Last modification date: 2024-09-04)

Primary citation

Attia, B.,My, L.,Castaing, J.P.,Dinet, C.,Le Guenno, H.,Schmidt, V.,Espinosa, L.,Anantharaman, V.,Aravind, L.,Sebban-Kreuzer, C.,Nouailler, M.,Bornet, O.,Viollier, P.,Elantak, L.,Mignot, T.
A molecular switch controls assembly of bacterial focal adhesions.
Sci Adv, 10:eadn2789-eadn2789, 2024

PubMed Abstract: Cell motility universally relies on spatial regulation of focal adhesion complexes (FAs) connecting the substrate to cellular motors. In bacterial FAs, the Adventurous gliding motility machinery (Agl-Glt) assembles at the leading cell pole following a Mutual gliding-motility protein (MglA)-guanosine 5'-triphosphate (GTP) gradient along the cell axis. Here, we show that GltJ, a machinery membrane protein, contains cytosolic motifs binding MglA-GTP and AglZ and recruiting the MreB cytoskeleton to initiate movement toward the lagging cell pole. In addition, MglA-GTP binding triggers a conformational shift in an adjacent GltJ zinc-finger domain, facilitating MglB recruitment near the lagging pole. This prompts GTP hydrolysis by MglA, leading to complex disassembly. The GltJ switch thus serves as a sensor for the MglA-GTP gradient, controlling FA activity spatially.

PubMed: 38809974
DOI: 10.1126/sciadv.adn2789

Experimental method

SOLUTION NMR