7ZOK
Solution structure of GltJ ZnR domain from Myxococcus xanthus
Summary for 7ZOK
| Entry DOI | 10.2210/pdb7zok/pdb |
| Related | 7Z3C |
| NMR Information | BMRB: 51104 |
| Descriptor | Adventurous gliding motility protein X, ZINC ION (2 entities 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 | 5845.21 |
| Authors | Attia, B.,My, L.,Castaing, J.P.,Le Guenno, H.,Espinosa, L.,Schmidt, V.,Nouailler, M.,Bornet, O.,Mignot, T.,Elantak, L. (deposition date: 2022-04-25, 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 Cited by 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: 38809974DOI: 10.1126/sciadv.adn2789 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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