6swz

Structure of the C-terminal domain of C. glutamicum mycoloyltransferase A

spinqualitylabelsall models 6swz, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6swz is a 1 chain structure with sequence from "micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL Gene: csp1, cop1, Cgl2875, cg3182 ("Micrococcus glutamicus" Kinoshita et al. 1958) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CSP1_CORGL] One of the two major secreted proteins. Publication Abstract from PubMed The genomes of Corynebacteriales contain several genes encoding mycoloyltransferases (Myt) that are specific cell envelope enzymes essential for the biogenesis of the outer membrane. MytA is a major mycoloyltransferase of Corynebacterium glutamicum, displaying an N-terminal domain with esterase activity and a C-terminal extension containing a conserved repeated LGFP sequence motif of unknown function. This motif is highly conserved in Corynebacteriales and found associated with cell wall hydrolases and with proteins of unknown function. In this study, we determined the crystal structure of MytA and found that its C-terminal domain is composed of five LGFP motifs and forms a long stalk perpendicular to the N-terminal catalytic alpha/beta-hydrolase domain. The LGFP motifs are composed of a 4-stranded beta-fold and occupy alternating orientations along the axis of the stalk. Multiple acetate binding pockets were identified in the stalk, which could correspond to putative ligand binding sites. By using various MytA mutants and complementary in vitro and in vivo approaches, we provide evidence that the C-terminal LGFP domain interacts with the cell wall peptidoglycan-arabinogalactan polymer. We also show that the C-terminal LGFP domain is not required for the activity of MytA but rather contributes to the overall integrity of the cell envelope. The C-terminal domain of Corynebacterium glutamicum mycoloyltransferase A is composed of five repeated motifs involved in cell wall binding and stability.,Dietrich C, Li de la Sierra-Gallay I, Masi M, Girard E, Dautin N, Constantinesco-Becker F, Tropis M, Daffe M, van Tilbeurgh H, Bayan N Mol Microbiol. 2020 Feb 19. doi: 10.1111/mmi.14492. PMID:32073722 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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