1kdg: Difference between revisions
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New page: left|200px<br /><applet load="1kdg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kdg, resolution 1.50Å" /> '''Crystal structure of... |
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== | ==Crystal structure of the flavin domain of cellobiose dehydrogenase== | ||
Cellobiose dehydrogenase (CDH) participates in the degradation of | <StructureSection load='1kdg' size='340' side='right'caption='[[1kdg]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1kdg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia 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 [https://proteopedia.org/fgij/fg.htm?mol=1KDG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></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=1kdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kdg OCA], [https://pdbe.org/1kdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kdg RCSB], [https://www.ebi.ac.uk/pdbsum/1kdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kdg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CDH_PHACH CDH_PHACH] Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone. | |||
== 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/initialview03.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/main_output.php?pdb_ID=1kdg 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1kdg" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Divne | <references/> | ||
[[Category: Hallberg | __TOC__ | ||
[[Category: Henriksson | </StructureSection> | ||
[[Category: Pettersson | [[Category: Large Structures]] | ||
[[Category: Phanerodontia chrysosporium]] | |||
[[Category: Divne C]] | |||
[[Category: Hallberg BM]] | |||
[[Category: Henriksson G]] | |||
[[Category: Pettersson G]] | |||
