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PDBsum entry 3wlm
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References listed in PDB file
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Key reference
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Title
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Discovery of processive catalysis by an exo-Hydrolase with a pocket-Shaped active site.
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Authors
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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.
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Ref.
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Nat Commun, 2019,
10,
2222.
[DOI no: ]
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PubMed id
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Abstract
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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.
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