5aa7: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa7 OCA], [http://pdbe.org/5aa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa7 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa7 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa7 OCA], [http://pdbe.org/5aa7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa7 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A resolution structure revealed deletions of interacting loops that protrude from the core beta-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. | |||
Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans.,Mekasha S, Forsberg Z, Dalhus B, Bacik JP, Choudhary S, Schmidt-Dannert C, Vaaje-Kolstad G, Eijsink VG FEBS Lett. 2016 Jan;590(1):34-42. doi: 10.1002/1873-3468.12025. Epub 2015 Dec 28. PMID:26763108<ref>PMID:26763108</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5aa7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 21:43, 27 January 2016
Structural and functional characterization of a chitin-active 15.5 kDa lytic polysaccharide monooxygenase domain from a modular chitinase from Jonesia denitrificansStructural and functional characterization of a chitin-active 15.5 kDa lytic polysaccharide monooxygenase domain from a modular chitinase from Jonesia denitrificans
Structural highlights
Publication Abstract from PubMedLytic 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 A resolution structure revealed deletions of interacting loops that protrude from the core beta-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. Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans.,Mekasha S, Forsberg Z, Dalhus B, Bacik JP, Choudhary S, Schmidt-Dannert C, Vaaje-Kolstad G, Eijsink VG FEBS Lett. 2016 Jan;590(1):34-42. doi: 10.1002/1873-3468.12025. Epub 2015 Dec 28. PMID:26763108[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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