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| | <StructureSection load='5tkf' size='340' side='right'caption='[[5tkf]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5tkf' size='340' side='right'caption='[[5tkf]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tkf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysonilia_crassa Chrysonilia 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TKF FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tki|5tki]], [[5tkh|5tkh]], [[5tkg|5tkg]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">G15G9.090, GE21DRAFT_7469 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5141 Chrysonilia crassa])</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> |
| - | <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=5tkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tkf OCA], [http://pdbe.org/5tkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tkf RCSB], [http://www.ebi.ac.uk/pdbsum/5tkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tkf ProSAT]</span></td></tr> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chrysonilia crassa]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dell, W B.O]] | + | [[Category: Neurospora crassa]] |
| - | [[Category: Meilleur, F]] | + | [[Category: Meilleur F]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: O'Dell WB]] |
| - | [[Category: Polysaccharide monooxygenase]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4]
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[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Phillips CM, Beeson WT, Cate JH, Marletta MA. Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol. 2011 Dec 16;6(12):1399-406. PMID:22004347 doi:10.1021/cb200351y
- ↑ Beeson WT, Phillips CM, Cate JH, Marletta MA. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J Am Chem Soc. 2012 Jan 18;134(2):890-2. PMID:22188218 doi:10.1021/ja210657t
- ↑ Vu VV, Beeson WT, Phillips CM, Cate JH, Marletta MA. Determinants of regioselective hydroxylation in the fungal polysaccharide monooxygenases. J Am Chem Soc. 2014 Jan 15;136(2):562-5. PMID:24350607 doi:10.1021/ja409384b
- ↑ Petrovic DM, Varnai A, Dimarogona M, Mathiesen G, Sandgren M, Westereng B, Eijsink VGH. Comparison of three seemingly similar lytic polysaccharide monooxygenases from Neurospora crassa suggests different roles in plant biomass degradation. J Biol Chem. 2019 Oct 11;294(41):15068-15081. doi: 10.1074/jbc.RA119.008196. Epub, 2019 Aug 20. PMID:31431506 doi:http://dx.doi.org/10.1074/jbc.RA119.008196
- ↑ O'Dell WB, Swartz PD, Weiss KL, Meilleur F. Crystallization of a fungal lytic polysaccharide monooxygenase expressed from glycoengineered Pichia pastoris for X-ray and neutron diffraction. Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):70-78. doi:, 10.1107/S2053230X16020318. Epub 2017 Jan 19. PMID:28177316 doi:http://dx.doi.org/10.1107/S2053230X16020318
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