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4qi3

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<StructureSection load='4qi3' size='340' side='right'caption='[[4qi3]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='4qi3' size='340' side='right'caption='[[4qi3]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qi3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_22112 Atcc 22112]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QI3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QI3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4qi3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crassicarpon_hotsonii Crassicarpon hotsonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QI3 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qi4|4qi4]], [[4qi5|4qi5]], [[4qi6|4qi6]], [[4qi7|4qi7]], [[4qi8|4qi8]]</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=4qi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qi3 OCA], [https://pdbe.org/4qi3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qi3 RCSB], [https://www.ebi.ac.uk/pdbsum/4qi3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qi3 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=455373 ATCC 22112])</td></tr>
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<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=4qi3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qi3 OCA], [http://pdbe.org/4qi3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qi3 RCSB], [http://www.ebi.ac.uk/pdbsum/4qi3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qi3 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A9XK88_9PEZI A9XK88_9PEZI]
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A new paradigm for cellulose depolymerization by fungi focuses on an oxidative mechanism involving cellobiose dehydrogenases (CDH) and copper-dependent lytic polysaccharide monooxygenases (LPMO); however, mechanistic studies have been hampered by the lack of structural information regarding CDH. CDH contains a haem-binding cytochrome (CYT) connected via a flexible linker to a flavin-dependent dehydrogenase (DH). Electrons are generated from cellobiose oxidation catalysed by DH and shuttled via CYT to LPMO. Here we present structural analyses that provide a comprehensive picture of CDH conformers, which govern the electron transfer between redox centres. Using structure-based site-directed mutagenesis, rapid kinetics analysis and molecular docking, we demonstrate that flavin-to-haem interdomain electron transfer (IET) is enabled by a haem propionate group and that rapid IET requires a closed CDH state in which the propionate is tightly enfolded by DH. Following haem reduction, CYT reduces LPMO to initiate oxygen activation at the copper centre and subsequent cellulose depolymerization.
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Structural basis for cellobiose dehydrogenase action during oxidative cellulose degradation.,Tan TC, Kracher D, Gandini R, Sygmund C, Kittl R, Haltrich D, Hallberg BM, Ludwig R, Divne C Nat Commun. 2015 Jul 7;6:7542. doi: 10.1038/ncomms8542. PMID:26151670<ref>PMID:26151670</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 4qi3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 22112]]
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[[Category: Crassicarpon hotsonii]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Divne, C]]
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[[Category: Divne C]]
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[[Category: Gandini, R]]
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[[Category: Gandini R]]
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[[Category: Hallberg, B M]]
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[[Category: Hallberg BM]]
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[[Category: Haltrich, D]]
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[[Category: Haltrich D]]
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[[Category: Kittl, R]]
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[[Category: Kittl R]]
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[[Category: Ludwig, R]]
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[[Category: Ludwig R]]
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[[Category: Sygmund, C]]
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[[Category: Sygmund C]]
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[[Category: Tan, T C]]
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[[Category: Tan TC]]
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[[Category: Cdh dehydrogenase domain]]
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[[Category: Electron transfer]]
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[[Category: Immunoglobulin-like beta-sandwich]]
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[[Category: Lpmo]]
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[[Category: Oxidoreductase]]
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Current revision

Cytochrome domain of Myriococcum thermophilum cellobiose dehydrogenase, MtCYT

PDB ID 4qi3

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