5tkf
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5tkf is ON HOLD Authors: O'Dell, W.B., Meilleur, F. Description: Neurospora crassa polysaccharide monooxygenase 2 high mannosylation [[Category: Un...) |
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- | '''Unreleased structure''' | ||
- | + | ==Neurospora crassa polysaccharide monooxygenase 2 high mannosylation== | |
+ | <StructureSection load='5tkf' size='340' side='right'caption='[[5tkf]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5tkf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa Neurospora crassa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TKF 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]] 2.1Å</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=5tkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tkf OCA], [https://pdbe.org/5tkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tkf RCSB], [https://www.ebi.ac.uk/pdbsum/5tkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tkf ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/LPMO_NEUCR LPMO_NEUCR] Catalyzes the oxidative cleavage of glycosidic bonds in cellulosic substrates via a copper-dependent mechanism (PubMed:22004347, PubMed:22188218, PubMed:24350607, PubMed:31431506). In the presence of an exogenous reductant ascorbic acid, degrades phosphoric acid swollen cellulose (PASC) to cello-oligosaccharides and 4-ketoaldoses, the end products oxidized at the non-reducing end (PubMed:22004347, PubMed:22188218, PubMed:24350607). Somewhat active toward tamarind xyloglucan and konjac glucomannan, with improved activity with glucomannan in the presence of PASC (PubMed:31431506). H(2)O(2) is able to substitute for O(2) in reactions with PASC, xyloglucan and glucomannan (PubMed:31431506). Very weak activity on cellopentaose (PubMed:31431506). No activity with birchwood xylan or ivory nut mannan (PubMed:31431506). Disrupts plant cell wall polysaccharide substrates, such as recalcitrant crystalline cellulose (Probable).<ref>PMID:22004347</ref> <ref>PMID:22188218</ref> <ref>PMID:24350607</ref> <ref>PMID:31431506</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Lytic polysaccharide monooxygenases (LPMOs) are carbohydrate-disrupting enzymes secreted by bacteria and fungi that break glycosidic bonds via an oxidative mechanism. Fungal LPMOs typically act on cellulose and can enhance the efficiency of cellulose-hydrolyzing enzymes that release soluble sugars for bioethanol production or other industrial uses. The enzyme PMO-2 from Neurospora crassa (NcPMO-2) was heterologously expressed in Pichia pastoris to facilitate crystallographic studies of the fungal LPMO mechanism. Diffraction resolution and crystal morphology were improved by expressing NcPMO-2 from a glycoengineered strain of P. pastoris and by the use of crystal seeding methods, respectively. These improvements resulted in high-resolution (1.20 A) X-ray diffraction data collection at 100 K and the production of a large NcPMO-2 crystal suitable for room-temperature neutron diffraction data collection to 2.12 A resolution. | ||
- | + | Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction.,O'Dell WB, Swartz PD, Weiss KL, Meilleur F Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):70-78. doi:, 10.1107/S2053230X16020318. Epub 2017 Jan 19. PMID:28177316<ref>PMID:28177316</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: Meilleur | + | <div class="pdbe-citations 5tkf" style="background-color:#fffaf0;"></div> |
- | [[Category: O'Dell | + | |
+ | ==See Also== | ||
+ | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Neurospora crassa]] | ||
+ | [[Category: Meilleur F]] | ||
+ | [[Category: O'Dell WB]] |
Current revision
Neurospora crassa polysaccharide monooxygenase 2 high mannosylation
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