3wlh › Citations

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

Fig. 1
Fig. 2
Fig. 3
Streltsov VA, Luang S, Peisley A, Varghese JN, Ketudat Cairns JR, Fort S, Hijnen M, Tvaroška I, Ardá A, Jiménez-Barbero J, Alfonso-Prieto M, Rovira C, Mendoza F, Tiessler-Sala L, Sánchez-Aparicio JE, Rodríguez-Guerra J, Lluch JM, Maréchal JD, Masgrau L, Hrmova M
OpenAccess logo Nat Commun 10 2222 (2019)
Related entries: 3wli, 3wlj, 3wlk, 3wll, 3wlm, 3wln, 3wlo, 3wlp, 3wlq, 3wlr, 6md6, 6mi1

Cited: 11 times
EuropePMC logo PMID: 31110237

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.

Articles - 3wlh mentioned but not cited (4)

  1. Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site. Streltsov VA, Luang S, Peisley A, Varghese JN, Ketudat Cairns JR, Fort S, Hijnen M, Tvaroška I, Ardá A, Jiménez-Barbero J, Alfonso-Prieto M, Rovira C, Mendoza F, Tiessler-Sala L, Sánchez-Aparicio JE, Rodríguez-Guerra J, Lluch JM, Maréchal JD, Masgrau L, Hrmova M. Nat Commun 10 2222 (2019)
  2. Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253. Ara KZG, Månberger A, Gabriško M, Linares-Pastén JA, Jasilionis A, Friðjónsson ÓH, Hreggviðsson GÓ, Janeček Š, Nordberg Karlsson E. Sci Rep 10 1329 (2020)
  3. The evolutionary advantage of an aromatic clamp in plant family 3 glycoside exo-hydrolases. Luang S, Fernández-Luengo X, Nin-Hill A, Streltsov VA, Schwerdt JG, Alonso-Gil S, Ketudat Cairns JR, Pradeau S, Fort S, Maréchal JD, Masgrau L, Rovira C, Hrmova M. Nat Commun 13 5577 (2022)
  4. Enzymes in 3D: Synthesis, remodelling, and hydrolysis of cell wall (1,3;1,4)-β-glucans. Hrmova M, Zimmer J, Bulone V, Fincher GB. Plant Physiol 194 33-50 (2023)


Reviews citing this publication (2)

  1. Research progress and the biotechnological applications of multienzyme complex. Jiang Y, Zhang X, Yuan H, Huang D, Wang R, Liu H, Wang T. Appl Microbiol Biotechnol 105 1759-1777 (2021)
  2. Drug Design in the Exascale Era: A Perspective from Massively Parallel QM/MM Simulations. Raghavan B, Paulikat M, Ahmad K, Callea L, Rizzi A, Ippoliti E, Mandelli D, Bonati L, De Vivo M, Carloni P. J Chem Inf Model 63 3647-3658 (2023)

Articles citing this publication (5)

  1. GPathFinder: Identification of Ligand-Binding Pathways by a Multi-Objective Genetic Algorithm. Sánchez-Aparicio JE, Sciortino G, Herrmannsdoerfer DV, Chueca PO, Pedregal JR, Maréchal JD. Int J Mol Sci 20 E3155 (2019)
  2. Molecular mechanisms of processive glycoside hydrolases underline catalytic pragmatism. Hrmova M, Schwerdt JG. Biochem Soc Trans 51 1387-1403 (2023)
  3. Tuning Selectivity in CalA Lipase: Beyond Tunnel Engineering. Alejaldre L, Lemay-St-Denis C, Pelletier JN, Quaglia D. Biochemistry 62 396-409 (2023)
  4. Geometric Remodeling of Nitrilase Active Pocket Based on ALF-Scanning Strategy To Enhance Aromatic Nitrile Substrate Preference and Catalytic Efficiency. Wang ZK, Gong JS, Feng DT, Su C, Li H, Rao ZM, Lu ZM, Shi JS, Xu ZH. Appl Environ Microbiol 89 e0022023 (2023)
  5. The Discovery of the Fucoidan-Active Endo-1→4-α-L-Fucanase of the GH168 Family, Which Produces Fucoidan Derivatives with Regular Sulfation and Anticoagulant Activity. Silchenko AS, Taran IV, Usoltseva RV, Zvyagintsev NV, Zueva AO, Rubtsov NK, Lembikova DE, Nedashkovskaya OI, Kusaykin MI, Isaeva MP, Ermakova SP. Int J Mol Sci 25 218 (2023)


Quick links