View source for 5n05


==X-ray crystal structure of an LPMO==
<StructureSection load='5n05' size='340' side='right'caption='[[5n05]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5n05]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Panus_similis Panus similis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5N05 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900020:beta-cellohexaose'>PRD_900020</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5n05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n05 OCA], [https://pdbe.org/5n05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5n05 RCSB], [https://www.ebi.ac.uk/pdbsum/5n05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5n05 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0S2GKZ1_9APHY A0A0S2GKZ1_9APHY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged.

Unliganded and substrate bound structures of the cellooligosaccharide active lytic polysaccharide monooxygenase LsAA9A at low pH.,Frandsen KEH, Poulsen JN, Tandrup T, Lo Leggio L Carbohydr Res. 2017 Aug 7;448:187-190. doi: 10.1016/j.carres.2017.03.010. Epub, 2017 Mar 24. PMID:28364950<ref>PMID:28364950</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5n05" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Panus similis]]
[[Category: Frandsen KEH]]
[[Category: Lo Leggio L]]
[[Category: Poulsen J-CN]]