3WLQ
Crystal Structure Analysis of Plant Exohydrolase
Summary for 3WLQ
| Entry DOI | 10.2210/pdb3wlq/pdb |
| Related | 1EX1 1IEQ 1IEV 1IEW 1IEX 1J8V 3WLH 3WLI 3WLJ 3WLK 3WLL 3WLM 3WLN 3WLO 3WLP 3WLR 3WLS 3WLT |
| Descriptor | Beta-D-glucan exohydrolase isoenzyme ExoI, 2-acetamido-2-deoxy-beta-D-glucopyranose, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | beta barrel, hydrolase, grain development, enzyme function initiative, tim barrel/beta sheet, n-glycosylation, plant apoplast |
| Biological source | Hordeum vulgare subsp. vulgare (barley,two-rowed barley) |
| Total number of polymer chains | 1 |
| Total formula weight | 67150.29 |
| Authors | Streltsov, V.A.,Luang, S.,Hrmova, M. (deposition date: 2013-11-12, release date: 2015-03-25, Last modification date: 2024-10-30) |
| Primary citation | Streltsov, V.A.,Luang, S.,Peisley, A.,Varghese, J.N.,Ketudat Cairns, J.R.,Fort, S.,Hijnen, M.,Tvaroska, I.,Arda, A.,Jimenez-Barbero, J.,Alfonso-Prieto, M.,Rovira, C.,Mendoza, F.,Tiessler-Sala, L.,Sanchez-Aparicio, J.E.,Rodriguez-Guerra, J.,Lluch, J.M.,Marechal, J.D.,Masgrau, L.,Hrmova, M. Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site. Nat Commun, 10:2222-2222, 2019 Cited by PubMed 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. PubMed: 31110237DOI: 10.1038/s41467-019-09691-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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