6SX4

Structure of C. glutamicum mycoloyltransferase A

これはPDB形式変換不可エントリーです。

6SX4 の概要

• エントリーDOI: 10.2210/pdb6sx4/pdb
• 関連するPDBエントリー: 6SWZ
• 分子名称: Protein PS1, ACETATE ION (3 entities in total)
• 機能のキーワード: mycoloyltransferase, transferase, mycolic acid, cell wall
• 由来する生物種: Corynebacterium glutamicum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 271514.35

構造登録者

Li de la Sierra-Gallay, I.,Van tilbeurgh, H.,Bayan, N. (登録日: 2019-09-24, 公開日: 2020-03-04, 最終更新日: 2024-10-23)

主引用文献

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

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: 32073722
DOI: 10.1111/mmi.14492

実験手法

X-RAY DIFFRACTION (2.796 Å)