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{{STRUCTURE_1kdg| PDB=1kdg | SCENE= }}
==Crystal structure of the flavin domain of cellobiose dehydrogenase==
===Crystal structure of the flavin domain of cellobiose dehydrogenase===
<StructureSection load='1kdg' size='340' side='right' caption='[[1kdg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
{{ABSTRACT_PUBMED_11786022}}
== Structural highlights ==
<table><tr><td colspan='2'>[[1kdg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KDG FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6FA:6-HYDROXY-FLAVIN-ADENINE+DINUCLEOTIDE'>6FA</scene>, <scene name='pdbligand=EMT:2-(ETHYLMERCURI-THIO)-BENZOIC+ACID'>EMT</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d7b|1d7b]], [[1d7c|1d7c]], [[1d7d|1d7d]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellobiose_dehydrogenase_(acceptor) Cellobiose dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.18 1.1.99.18] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kdg RCSB], [http://www.ebi.ac.uk/pdbsum/1kdg PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/1kdg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cellobiose dehydrogenase (CDH) participates in the degradation of cellulose and lignin. The protein is an extracellular flavocytochrome with a b-type cytochrome domain (CYT(cdh)) connected to a flavodehydrogenase domain (DH(cdh)). DH(cdh) catalyses a two-electron oxidation at the anomeric C1 position of cellobiose to yield cellobiono-1,5-lactone, and the electrons are subsequently transferred from DH(cdh) to an acceptor, either directly or via CYT(cdh). Here, we describe the crystal structure of Phanerochaete chrysosporium DH(cdh) determined at 1.5 A resolution. DH(cdh) belongs to the GMC family of oxidoreductases, which includes glucose oxidase (GOX) and cholesterol oxidase (COX); however, the sequence identity with members of the family is low. The overall fold of DH(cdh) is p-hydroxybenzoate hydroxylase-like and is similar to, but also different from, that of GOX and COX. It is partitioned into an FAD-binding subdomain of alpha/beta type and a substrate-binding subdomain consisting of a seven-stranded beta sheet and six helices. Docking of CYT(cdh) and DH(cdh) suggests that CYT(cdh) covers the active-site entrance in DH(cdh), and that the resulting distance between the cofactors is within acceptable limits for inter-domain electron transfer. Based on docking of the substrate, cellobiose, in the active site of DH(cdh), we propose that the enzyme discriminates against glucose by favouring interaction with the non-reducing end of cellobiose.


==Function==
Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase.,Hallberg BM, Henriksson G, Pettersson G, Divne C J Mol Biol. 2002 Jan 18;315(3):421-34. PMID:11786022<ref>PMID:11786022</ref>
[[http://www.uniprot.org/uniprot/CDH_PHACH CDH_PHACH]] Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[1kdg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KDG OCA].
</div>
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:011786022</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Phanerochaete chrysosporium]]
[[Category: Phanerochaete chrysosporium]]
[[Category: Divne, C.]]
[[Category: Divne, C.]]
Retrieved from "https://proteopedia.org/1kdg"