5tkf: Difference between revisions
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==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. 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> | |||
</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> | |||
<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='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> | |||
<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> | ||
<div class="pdbe-citations 5tkf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Dell, W B.O]] | |||
[[Category: Meilleur, F]] | [[Category: Meilleur, F]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
[[Category: Polysaccharide monooxygenase]] | |||
Revision as of 18:44, 17 May 2017
Neurospora crassa polysaccharide monooxygenase 2 high mannosylationNeurospora crassa polysaccharide monooxygenase 2 high mannosylation
Structural highlights
Publication Abstract from PubMedLytic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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