3qde

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Current revision (10:47, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3qde' size='340' side='right'caption='[[3qde]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3qde' size='340' side='right'caption='[[3qde]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qde]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qde]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbp, Q8VP44 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 "Ruminiclostridium thermocellum" Yutin and Galperin 2013])</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=144:TRIS-HYDROXYMETHYL-METHYL-AMMONIUM'>144</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellobiose_phosphorylase Cellobiose phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.20 2.4.1.20] </span></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=3qde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qde OCA], [https://pdbe.org/3qde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qde RCSB], [https://www.ebi.ac.uk/pdbsum/3qde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qde 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=3qde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qde OCA], [https://pdbe.org/3qde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qde RCSB], [https://www.ebi.ac.uk/pdbsum/3qde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qde ProSAT]</span></td></tr>
</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/Q8VP44_ACETH Q8VP44_ACETH]
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Clostridium thermocellum is a cellulosome-producing bacterium that is able to efficiently degrade and utilize cellulose as a sole carbon source. Cellobiose phosphorylase (CBP) plays a critical role in cellulose degradation by catalyzing the reversible phosphate-dependent hydrolysis of cellobiose, the major product of cellulose degradation, into alpha-D-glucose 1-phosphate and D-glucose. CBP from C. thermocellum is a modular enzyme composed of four domains [N-terminal domain, helical linker, (alpha/alpha)(6)-barrel domain and C-terminal domain] and is a member of glycoside hydrolase family 94. The 2.4 A resolution X-ray crystal structure of C. thermocellum CBP reveals the residues involved in coordinating the catalytic phosphate as well as the residues that are likely to be involved in substrate binding and discrimination.
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Structure of cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate.,Bianchetti CM, Elsen NL, Fox BG, Phillips GN Jr Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Nov 1;67(Pt 11):1345-9., Epub 2011 Oct 25. PMID:22102229<ref>PMID:22102229</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 3qde" 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: Ruminiclostridium thermocellum yutin and galperin 2013]]
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[[Category: Acetivibrio thermocellus]]
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[[Category: Cellobiose phosphorylase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bianchetti, C M]]
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[[Category: Bianchetti CM]]
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[[Category: Elsen, N L]]
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[[Category: Elsen NL]]
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[[Category: Fox, B G]]
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[[Category: Fox BG]]
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[[Category: Horn, M K]]
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[[Category: Horn MK]]
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[[Category: Phillips, G N]]
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[[Category: Phillips Jr GN]]
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[[Category: Cellobiose]]
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[[Category: Cellulase]]
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[[Category: Phosphate]]
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[[Category: Phosphorylase]]
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[[Category: Transferase]]
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Current revision

The structure of Cellobiose phosphorylase from Clostridium thermocellum in complex with phosphate

PDB ID 3qde

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