4U6D

Zg3615, a family 117 glycoside hydrolase in complex with beta-3,6-anhydro-L-galactose

4U6D の概要

• エントリーDOI: 10.2210/pdb4u6d/pdb
• 分子名称: Conserved hypothetical periplasmic protein, CALCIUM ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• 機能のキーワード: gh117, hydrolase, bicyclic sugar
• 由来する生物種: Zobellia galactanivorans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96796.34

構造登録者

Ficko-Blean, E. (登録日: 2014-07-28, 公開日: 2015-02-11, 最終更新日: 2023-12-20)

主引用文献

Ficko-Blean, E.,Duffieux, D.,Rebuffet, E.,Larocque, R.,Groisillier, A.,Michel, G.,Czjzek, M.
Biochemical and structural investigation of two paralogous glycoside hydrolases from Zobellia galactanivorans: novel insights into the evolution, dimerization plasticity and catalytic mechanism of the GH117 family.
Acta Crystallogr.,Sect.D, 71:209-223, 2015

PubMed Abstract: The family 117 glycoside hydrolase (GH117) enzymes have exo-α-1,3-(3,6-anhydro)-L-galactosidase activity, removing terminal nonreducing α-1,3-linked 3,6-anhydro-L-galactose residues from their red algal neoagarose substrate. These enzymes have previously been phylogenetically divided into clades, and only the clade A enzymes have been experimentally studied to date. The investigation of two GH117 enzymes, Zg3615 and Zg3597, produced by the marine bacterium Zobellia galactanivorans reveals structural, biochemical and further phylogenetic diversity between clades. A product complex with the unusual β-3,6-anhydro-L-galactose residue sheds light on the inverting catalytic mechanism of the GH117 enzymes as well as the structure of this unique sugar produced by hydrolysis of the agarophyte red algal cell wall.

PubMed: 25664732
DOI: 10.1107/S1399004714025024

実験手法

X-RAY DIFFRACTION (1.7 Å)