7pxt

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==Structure of an LPMO, collected from serial synchrotron crystallography data.==
==Structure of an LPMO, collected from serial synchrotron crystallography data.==
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<StructureSection load='7pxt' size='340' side='right'caption='[[7pxt]]' scene=''>
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<StructureSection load='7pxt' size='340' side='right'caption='[[7pxt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PXT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7pxt]] 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=7PXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PXT FirstGlance]. <br>
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</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=7pxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pxt OCA], [https://pdbe.org/7pxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pxt RCSB], [https://www.ebi.ac.uk/pdbsum/7pxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pxt ProSAT]</span></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7pxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pxt OCA], [https://pdbe.org/7pxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pxt RCSB], [https://www.ebi.ac.uk/pdbsum/7pxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pxt ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/A0A0S2GKZ1_9APHY A0A0S2GKZ1_9APHY]]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The recently discovered lytic polysaccharide monooxygenases (LPMOs) are Cu-containing enzymes capable of degrading polysaccharide substrates oxidatively. The generally accepted first step in the LPMO reaction is the reduction of the active-site metal ion from Cu(2+) to Cu(+). Here we have used a systematic diffraction data collection method to monitor structural changes in two AA9 LPMOs, one from Lentinus similis (LsAA9_A) and one from Thermoascus auranti-acus (TaAA9_A), as the active-site Cu is photoreduced in the X-ray beam. For LsAA9_A, the protein produced in two different recombinant systems was crystallized to probe the effect of post-translational modifications and different crystallization conditions on the active site and metal photoreduction. We can recommend that crystallographic studies of AA9 LPMOs wishing to address the Cu(2+) form use a total X-ray dose below 3 x 10(4) Gy, while the Cu(+) form can be attained using 1 x 10(6) Gy. In all cases, we observe the transition from a hexa-coordinated Cu site with two solvent-facing ligands to a T-shaped geometry with no exogenous ligands, and a clear increase of the theta2 parameter and a decrease of the theta3 parameter by averages of 9.2 degrees and 8.4 degrees , respectively, but also a slight increase in thetaT. Thus, the theta2 and theta3 parameters are helpful diagnostics for the oxidation state of the metal in a His-brace protein. On binding of cello-oligosaccharides to LsAA9_A, regardless of the production source, the thetaT parameter increases, making the Cu site less planar, while the active-site Tyr-Cu distance decreases reproducibly for the Cu(2+) form. Thus, the thetaT increase found on copper reduction may bring LsAA9_A closer to an oligosaccharide-bound state and contribute to the observed higher affinity of reduced LsAA9_A for cellulosic substrates.
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Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding.,Tandrup T, Muderspach SJ, Banerjee S, Santoni G, Ipsen JO, Hernandez-Rollan C, Norholm MHH, Johansen KS, Meilleur F, Lo Leggio L IUCrJ. 2022 Aug 17;9(Pt 5):666-681. doi: 10.1107/S2052252522007175. eCollection, 2022 Sep 1. PMID:36071795<ref>PMID:36071795</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7pxt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Panus similis]]
[[Category: Lo Leggio L]]
[[Category: Lo Leggio L]]
[[Category: Santoni G]]
[[Category: Santoni G]]
[[Category: Tandrup T]]
[[Category: Tandrup T]]

Revision as of 07:53, 21 September 2022

Structure of an LPMO, collected from serial synchrotron crystallography data.

PDB ID 7pxt

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