PDBsum entry 4zmh

Hydrolase

PDB id: 4zmh

Contents

Protein chains

935 a.a.

Ligands

PO4 ×4

GOL ×2

ACT

Metals

_NA ×2

Waters ×2181

PDB id:

4zmh

Name:

Hydrolase

Title:

Crystal structure of a five-domain gh115 alpha-glucuronidase from the marine bacterium saccharophagus degradans 2-40t

Structure:

Uncharacterized protein. Chain: a, b. Fragment: unp residues 37-975. Engineered: yes

Source:

Saccharophagus degradans. Organism_taxid: 203122. Strain: 2-40 / atcc 43961 / dsm 17024. Gene: sde_1755. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.93Å R-factor: 0.140 R-free: 0.170

Authors:

B.Nocek,H.Cui,W.Wang,A.Savchenko

Key ref:

W.Wang et al. (2016). Biochemical and Structural Characterization of a Five-domain GH115 α-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T. J Biol Chem, 291, 14120-14133. PubMed id: 27129264 DOI: 10.1074/jbc.M115.702944

Date:

04-May-15 Release date: 04-May-16

Protein chains

Q21JW4  (Q21JW4_SACD2) -  Gylcosyl hydrolase 115 C-terminal domain-containing protein from Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)

Seq: 975 a.a.

Struc: 935 a.a.

DOI no: 10.1074/jbc.M115.702944

J Biol Chem 291:14120-14133 (2016)

PubMed id: 27129264

Biochemical and Structural Characterization of a Five-domain GH115 α-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T.

W.Wang, R.Yan, B.P.Nocek, T.V.Vuong, R.Di Leo, X.Xu, H.Cui, P.Gatenholm, G.Toriz, M.Tenkanen, A.Savchenko, E.R.Master.

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.