View source for 5aa7


==Structural and functional characterization of a chitin-active 15.5 kDa lytic polysaccharide monooxygenase domain from a modular chitinase from Jonesia denitrificans==
<StructureSection load='5aa7' size='340' side='right' caption='[[5aa7]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5aa7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AA7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chitinase Chitinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.14 3.2.1.14] </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>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5aa7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chitinase]]
[[Category: Choudhary, S]]
[[Category: Dalhus, B]]
[[Category: Eijsink, V]]
[[Category: Forsberg, Z]]
[[Category: Mekasha, S]]
[[Category: Schmidt-Dannert, C]]
[[Category: Vaaje-Kolstad, G]]
[[Category: Hydrolase]]