6EHN

Structural insight into a promiscuous CE15 esterase from the marine bacterial metagenome

6EHN の概要

• エントリーDOI: 10.2210/pdb6ehn/pdb
• 分子名称: Carbohydrate esterase MZ0003, GLYCEROL (3 entities in total)
• 機能のキーワード: esterase, protein structure, hydrolase
• 由来する生物種: Unknown prokaryotic organism
• 細胞内の位置: Periplasm : A0A0K2VM55
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44981.92

構造登録者

Helland, R.,De Santi, C.,Gani, O.,Williamson, A.K. (登録日: 2017-09-13, 公開日: 2018-03-21, 最終更新日: 2024-05-08)

主引用文献

De Santi, C.,Gani, O.A.,Helland, R.,Williamson, A.
Structural insight into a CE15 esterase from the marine bacterial metagenome.
Sci Rep, 7:17278-17278, 2017

PubMed Abstract: The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial sub-clade. The catalytic triad of the bacterial CE15, which includes Asp 332 as its third member, closely resembles that of family 1 carbohydrate esterases (CE1), despite the overall lower structural similarity with members of this family. Two of the three loop regions form a subdomain that deepens the active site pocket and includes several basic residues that contribute to the high positive charge surrounding the active site. Docking simulations predict specific interactions with the sugar moiety of glucuronic-acid substrates, and with aromatically-substituted derivatives that serve as model compounds for the lignin-carbohydrate complex of plant cell walls. Molecular dynamics simulations indicate considerable flexibility of the sub-domain in the substrate-bound form, suggesting plasticity to accommodate different substrates is possible. The findings from this first reported structure of a bacterial member of the CE15 family provide insight into the basis of its broader substrate specificity.

PubMed: 29222424
DOI: 10.1038/s41598-017-17677-4

実験手法

X-RAY DIFFRACTION (1.9 Å)