4h7u: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:


==Crystal structure of pyranose dehydrogenase from Agaricus meleagris, wildtype==
==Crystal structure of pyranose dehydrogenase from Agaricus meleagris, wildtype==
<StructureSection load='4h7u' size='340' side='right' caption='[[4h7u]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4h7u' size='340' side='right'caption='[[4h7u]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4h7u]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Agaricus_meleagris Agaricus meleagris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H7U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H7U FirstGlance]. <br>
<table><tr><td colspan='2'>[[4h7u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leucoagaricus_meleagris Leucoagaricus meleagris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H7U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FED:[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl+(2R,3S,4S)-2,3,4-trihydroxy-5-[(4aR)-4a-hydroxy-7,8-dimethyl-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]pentyl+dihydrogen+diphosphate+(non-preferred+name)'>FED</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FED:[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl+(2R,3S,4S)-2,3,4-trihydroxy-5-[(4aR)-4a-hydroxy-7,8-dimethyl-2,4-dioxo-3,4,4a,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]pentyl+dihydrogen+diphosphate+(non-preferred+name)'>FED</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pdh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=201219 Agaricus meleagris])</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=4h7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h7u OCA], [https://pdbe.org/4h7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h7u RCSB], [https://www.ebi.ac.uk/pdbsum/4h7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h7u ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_dehydrogenase_(acceptor) Pyranose dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.29 1.1.99.29] </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=4h7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h7u OCA], [http://pdbe.org/4h7u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h7u RCSB], [http://www.ebi.ac.uk/pdbsum/4h7u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h7u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDH1_LEUMG PDH1_LEUMG] Catalyzes the single-oxidation or sequential double oxidation reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with the concomitant reduction of the flavin. The enzyme exhibits a broad sugar substrate specificity, oxidizing different aldopyranoses to the corresponding C-1, C-2, C-3 or C-1,2, C-2,3 and C-3,4 (di)dehydro sugars with substrate-specific regioselectivity. Accepts only a narrow range of electron acceptors such as substituted benzoquinones and complexed metal ions and reacts extremely slowly with O(2) as acceptor. May play a role in the natural recycling of plant matter by oxidizing all major monosaccharides in lignocellulose and by reducing quinone compounds or reactive radical species generated during lignin depolymerization.<ref>PMID:18083263</ref> <ref>PMID:18097667</ref> <ref>PMID:23326459</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 22: Line 22:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Agaricus meleagris]]
[[Category: Large Structures]]
[[Category: Divne, C]]
[[Category: Leucoagaricus meleagris]]
[[Category: Spadiut, O]]
[[Category: Divne C]]
[[Category: Tan, T C]]
[[Category: Spadiut O]]
[[Category: Fad binding]]
[[Category: Tan TC]]
[[Category: Flavin adduct]]
[[Category: Glycoprotein]]
[[Category: Gmc-oxidoreductase family]]
[[Category: Oxidoreductase]]
[[Category: Pyranose dehydrogenase]]
[[Category: Secreted]]