PDBsum entry 3wlm

Hydrolase

PDB id: 3wlm

Contents

Protein chain

602 a.a.

Ligands

NAG-NAG-BMA

NAG-NAG-BMA-FUC

NAG

BOG

Waters ×870

PDB id:

3wlm

Name:

Hydrolase

Title:

Crystal structure of barley beta-d-glucan glucohydrolase isoenzyme exo1 in complex with octyl-o-glucoside

Structure:

Beta-d-glucan exohydrolase isoenzyme exoi. Chain: a. Fragment: unp residues 26-630. Ec: 3.2.1.-

Source:

Hordeum vulgare subsp. Vulgare. Barley,two-rowed barley. Organism_taxid: 112509

Resolution:

1.90Å R-factor: 0.171 R-free: 0.201

Authors:

V.A.Streltsov,M.Hrmova

Key ref:

V.A.Streltsov et al. (2019). Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site. Nat Commun, 10, 2222. PubMed id: 31110237 DOI: 10.1038/s41467-019-09691-z

Date:

12-Nov-13 Release date: 25-Mar-15

Protein chain

Q9XEI3  (Q9XEI3_HORVV) -  beta-glucosidase from Hordeum vulgare subsp. vulgare

Seq: 630 a.a.

Struc: 602 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.2.1.21 - beta-glucosidase.
• Reaction: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.

DOI no: 10.1038/s41467-019-09691-z

Nat Commun 10:2222 (2019)

PubMed id: 31110237

Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.

V.A.Streltsov, S.Luang, A.Peisley, J.N.Varghese, J.R.Ketudat Cairns, S.Fort, M.Hijnen, I.Tvaroška, A.Ardá, J.Jiménez-Barbero, M.Alfonso-Prieto, C.Rovira, F.Mendoza, L.Tiessler-Sala, J.E.Sánchez-Aparicio, J.Rodríguez-Guerra, J.M.Lluch, J.D.Maréchal, L.Masgrau, M.Hrmova.

ABSTRACT

Substrates associate and products dissociate from enzyme catalytic sites rapidly, which hampers investigations of their trajectories. The high-resolution structure of the native Hordeum exo-hydrolase HvExoI isolated from seedlings reveals that non-covalently trapped glucose forms a stable enzyme-product complex. Here, we report that the alkyl β-D-glucoside and methyl 6-thio-β-gentiobioside substrate analogues perfused in crystalline HvExoI bind across the catalytic site after they displace glucose, while methyl 2-thio-β-sophoroside attaches nearby. Structural analyses and multi-scale molecular modelling of nanoscale reactant movements in HvExoI reveal that upon productive binding of incoming substrates, the glucose product modifies its binding patterns and evokes the formation of a transient lateral cavity, which serves as a conduit for glucose departure to allow for the next catalytic round. This path enables substrate-product assisted processive catalysis through multiple hydrolytic events without HvExoI losing contact with oligo- or polymeric substrates. We anticipate that such enzyme plasticity could be prevalent among exo-hydrolases.