4qi6: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4qi6]] is a 1 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=4QI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QI6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4qi6]] is a 1 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=4QI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QI6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=4qi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qi6 OCA], [https://pdbe.org/4qi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qi6 RCSB], [https://www.ebi.ac.uk/pdbsum/4qi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qi6 ProSAT]</span></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=4qi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qi6 OCA], [https://pdbe.org/4qi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qi6 RCSB], [https://www.ebi.ac.uk/pdbsum/4qi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qi6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/A9XK88_9PEZI A9XK88_9PEZI]  
[https://www.uniprot.org/uniprot/A9XK88_9PEZI A9XK88_9PEZI]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qi6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 09:52, 3 April 2024

Cellobiose dehydrogenase from Myriococcum thermophilum, MtCDHCellobiose dehydrogenase from Myriococcum thermophilum, MtCDH

Structural highlights

4qi6 is a 1 chain structure with sequence from Crassicarpon hotsonii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A9XK88_9PEZI

4qi6, resolution 3.20Å

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