Attia, Bouchra

Bornet, Olivier

Castaing, Jean-Philippe

Elantak, Latifa

Guerlesquin, Françoise

Mignot, Tâm

My, Laetitia

Serrano, Bastien

International audienceBacterial cell motility is essential for a range of physiological phenomena such as nutrient sensing, predation, biofilm formation and pathogenesis. One of the most intriguing motilities is bacterial gliding, which is defined as the ability of some bacteria to move across surfaces without an external appendage. In Myxococcus xanthus, gliding motility depends on the assembly of focal adhesion complexes (FAC) which include the Glt mutiprotein complex and allow directional movement of individual cells (A-motility). Within the Glt multiprotein complex, GltJ is one of the key proteins involved in FAC assembly. In this work we report complete backbone and side chain 1H, 13C and 15N chemical shifts of the two cytoplasmic domains of GltJ, GltJ-ZnR (BMRB No. 51104) and GltJ-GYF (BMRB No. 51096). These data provide the first step toward the first high resolution structures of protein domains from the Glt machinery and the atomic level characterization of GltJ cytoplasmic activity during FAC assembly

HAL AMU

1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus

1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus

Abstract

Similar works

Full text

Available Versions

HAL AMU