Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans

Sophanit Mekasha; Zarah Forsberg; Bjørn Dalhus; John Paul Bacik; Swati Choudhary; Claudia Schmidt-Dannert; Gustav Vaaje-Kolstad; Vincent G.H. Eijsink

doi:10.1002/1873-3468.12025

Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans

Sophanit Mekasha, Zarah Forsberg, Bjørn Dalhus, John Paul Bacik, Swati Choudhary, Claudia Schmidt-Dannert, Gustav Vaaje-Kolstad, Vincent G.H. Eijsink

Synthetic Biology and Biotechnology Division

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction.

Original language	English (US)
Pages (from-to)	34-42
Number of pages	9
Journal	FEBS Letters
Volume	590
Issue number	1
DOIs	https://doi.org/10.1002/1873-3468.12025
State	Published - Jan 1 2016

Bibliographical note

Funding Information:
This work was supported by The Research Council of Norway through grants 214138 and 221576 and by the Vista programme of the Norwegian Academy of Science and Letters (grant 6510). We are grateful for synchrotron travel support from The Research Council of Norway (216625/F50) and support from the South- Eastern Norway Regional Health Authority (Grants No. 2012085 and 2015095; Regional Core Facility for Structural Biology to BD). We also thank the European Synchrotron Radiation Facility staff for help and beamtime at beamline ID29 (project MX-1468).

Publisher Copyright:
© 2015 Federation of European Biochemical Societies.

Keywords

AA10
Jonesia denitrificans
chitin
chitinase
lytic polysaccharide monooxygenase

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10.1002/1873-3468.12025

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Mekasha, S., Forsberg, Z., Dalhus, B., Bacik, J. P., Choudhary, S., Schmidt-Dannert, C., Vaaje-Kolstad, G., & Eijsink, V. G. H. (2016). Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans. FEBS Letters, 590(1), 34-42. https://doi.org/10.1002/1873-3468.12025

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abstract = "Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 {\AA} resolution structure revealed deletions of interacting loops that protrude from the core β-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction.",

keywords = "AA10, Jonesia denitrificans, chitin, chitinase, lytic polysaccharide monooxygenase",

author = "Sophanit Mekasha and Zarah Forsberg and Bj{\o}rn Dalhus and Bacik, {John Paul} and Swati Choudhary and Claudia Schmidt-Dannert and Gustav Vaaje-Kolstad and Eijsink, {Vincent G.H.}",

note = "Funding Information: This work was supported by The Research Council of Norway through grants 214138 and 221576 and by the Vista programme of the Norwegian Academy of Science and Letters (grant 6510). We are grateful for synchrotron travel support from The Research Council of Norway (216625/F50) and support from the South- Eastern Norway Regional Health Authority (Grants No. 2012085 and 2015095; Regional Core Facility for Structural Biology to BD). We also thank the European Synchrotron Radiation Facility staff for help and beamtime at beamline ID29 (project MX-1468). Publisher Copyright: {\textcopyright} 2015 Federation of European Biochemical Societies.",

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doi = "10.1002/1873-3468.12025",

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AU - Forsberg, Zarah

AU - Dalhus, Bjørn

AU - Bacik, John Paul

AU - Choudhary, Swati

AU - Schmidt-Dannert, Claudia

AU - Vaaje-Kolstad, Gustav

AU - Eijsink, Vincent G.H.

N1 - Funding Information: This work was supported by The Research Council of Norway through grants 214138 and 221576 and by the Vista programme of the Norwegian Academy of Science and Letters (grant 6510). We are grateful for synchrotron travel support from The Research Council of Norway (216625/F50) and support from the South- Eastern Norway Regional Health Authority (Grants No. 2012085 and 2015095; Regional Core Facility for Structural Biology to BD). We also thank the European Synchrotron Radiation Facility staff for help and beamtime at beamline ID29 (project MX-1468). Publisher Copyright: © 2015 Federation of European Biochemical Societies.

PY - 2016/1/1

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N2 - Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction.

AB - Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction.

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Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans

Abstract

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Keywords

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