6SWZ
Structure of the C-terminal domain of C. glutamicum mycoloyltransferase A
This is a non-PDB format compatible entry.
Summary for 6SWZ
| Entry DOI | 10.2210/pdb6swz/pdb |
| Descriptor | Protein PS1, GLYCEROL (3 entities in total) |
| Functional Keywords | mycoloyltransferase, transferase, mycolic acid, cell wall |
| Biological source | Corynebacterium glutamicum |
| Total number of polymer chains | 1 |
| Total formula weight | 28412.86 |
| Authors | Li de la Sierra-Gallay, I.,Van tilbeurgh, H.,Bayan, N. (deposition date: 2019-09-24, release date: 2020-03-04, Last modification date: 2024-05-15) |
| Primary citation | 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. The C-terminal domain of Corynebacterium glutamicum mycoloyltransferase A is composed of five repeated motifs involved in cell wall binding and stability. Mol.Microbiol., 114:1-16, 2020 Cited by PubMed Abstract: 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 Leu-Gly-Phe-Pro (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 α/β-hydrolase domain. The LGFP motifs are composed of a 4-stranded β-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. PubMed: 32073722DOI: 10.1111/mmi.14492 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.995 Å) |
Structure validation
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