6GVB

Crystal structure of Cutibacterium acnes exo-beta-1,4-mannosidase

6GVB の概要

• エントリーDOI: 10.2210/pdb6gvb/pdb
• 分子名称: exo-beta-1,4-mannosidase, 3[N-MORPHOLINO]PROPANE SULFONIC ACID (3 entities in total)
• 機能のキーワード: exo-beta-1, 4-mannosidase, glycan degradation, enzyme, glycoside hydrolase, family 5, hydrolase
• 由来する生物種: Cutibacterium acnes (Propionibacterium acnes)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 189446.84

構造登録者

Reichenbach, T.,Divne, C. (登録日: 2018-06-20, 公開日: 2019-07-03, 最終更新日: 2024-05-15)

主引用文献

Reichenbach, T.,Kalyani, D.,Gandini, R.,Svartstrom, O.,Aspeborg, H.,Divne, C.
Structural and biochemical characterization of the Cutibacterium acnes exo-beta-1,4-mannosidase that targets the N-glycan core of host glycoproteins.
Plos One, 13:e0204703-e0204703, 2018

PubMed Abstract: Commensal and pathogenic bacteria have evolved efficient enzymatic pathways to feed on host carbohydrates, including protein-linked glycans. Most proteins of the human innate and adaptive immune system are glycoproteins where the glycan is critical for structural and functional integrity. Besides enabling nutrition, the degradation of host N-glycans serves as a means for bacteria to modulate the host's immune system by for instance removing N-glycans on immunoglobulin G. The commensal bacterium Cutibacterium acnes is a gram-positive natural bacterial species of the human skin microbiota. Under certain circumstances, C. acnes can cause pathogenic conditions, acne vulgaris, which typically affects 80% of adolescents, and can become critical for immunosuppressed transplant patients. Others have shown that C. acnes can degrade certain host O-glycans, however, no degradation pathway for host N-glycans has been proposed. To investigate this, we scanned the C. acnes genome and were able to identify a set of gene candidates consistent with a cytoplasmic N-glycan-degradation pathway of the canonical eukaryotic N-glycan core. We also found additional gene sequences containing secretion signals that are possible candidates for initial trimming on the extracellular side. Furthermore, one of the identified gene products of the cytoplasmic pathway, AEE72695, was produced and characterized, and found to be a functional, dimeric exo-β-1,4-mannosidase with activity on the β-1,4 glycosidic bond between the second N-acetylglucosamine and the first mannose residue in the canonical eukaryotic N-glycan core. These findings corroborate our model of the cytoplasmic part of a C. acnes N-glycan degradation pathway.

PubMed: 30261037
DOI: 10.1371/journal.pone.0204703

実験手法

X-RAY DIFFRACTION (1.8 Å)