4ZMH

Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T

4ZMH の概要

• エントリーDOI: 10.2210/pdb4zmh/pdb
• 分子名称: Uncharacterized protein, PHOSPHATE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: glycosyl hydrolase, hydrolase
• 由来する生物種: Saccharophagus degradans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 214977.50

構造登録者

Nocek, B.,Cui, H.,Wang, W.,Savchenko, A. (登録日: 2015-05-04, 公開日: 2016-05-04, 最終更新日: 2024-11-06)

主引用文献

Wang, W.,Yan, R.,Nocek, B.P.,Vuong, T.V.,Di Leo, R.,Xu, X.,Cui, H.,Gatenholm, P.,Toriz, G.,Tenkanen, M.,Savchenko, A.,Master, E.R.
Biochemical and Structural Characterization of a Five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T.
J.Biol.Chem., 291:14120-14133, 2016

PubMed Abstract: Glucuronic acid (GlcAp) and/or methylglucuronic acid (MeGlcAp) decorate the major forms of xylan in hardwood and coniferous softwoods as well as many cereal grains. Accordingly, the complete utilization of glucuronoxylans or conversion to sugar precursors requires the action of main chain xylanases as well as α-glucuronidases that release the α- (1→2)-linked (Me)GlcAp side groups. Herein, a family GH115 enzymefrom the marine bacterium Saccharophagus degradans 2-40(T), SdeAgu115A, demonstrated activity toward glucuronoxylan and oligomers thereof with preference toward MeGlcAp linked to internal xylopyranosyl residues. Unique biochemical characteristics of NaCl activation were also observed. The crystal structure of SdeAgu115A revealed a five-domain architecture, with an additional insertion C(+) domain that had significant impact on the domain arrangement of SdeAgu115A monomer and its dimerization. The participation of domain C(+) in substrate binding was supported by reduced substrate inhibition upon introducing W773A, W689A, and F696A substitutions within this domain. In addition to Asp-335, the catalytic essentiality of Glu-216 was revealed by site-specific mutagenesis. A primary sequence analysis suggested that the SdeAgu115A architecture is shared by more than half of GH115 members, thus defining a distinct archetype for GH115 enzymes.

PubMed: 27129264
DOI: 10.1074/jbc.M115.702944

実験手法

X-RAY DIFFRACTION (1.93 Å)