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3vgi

From Proteopedia

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Current revision (08:39, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3vgi' size='340' side='right'caption='[[3vgi]], [[Resolution|resolution]] 1.07&Aring;' scene=''>
<StructureSection load='3vgi' size='340' side='right'caption='[[3vgi]], [[Resolution|resolution]] 1.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VGI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vgi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VGI 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</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]] 1.07&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3az0|3az0]]</div></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eglA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</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=3vgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgi OCA], [https://pdbe.org/3vgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vgi RCSB], [https://www.ebi.ac.uk/pdbsum/3vgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vgi 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=3vgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgi OCA], [https://pdbe.org/3vgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vgi RCSB], [https://www.ebi.ac.uk/pdbsum/3vgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vgi 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/Q9V2T0_9EURY Q9V2T0_9EURY]
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Hyperthermophilic glycoside hydrolase family 12 endocellulase (EGPf) from the archaeon Pyrococcus furiosus catalyzes the hydrolytic cleavage of beta-1,4-glucosidic linkage in beta-glucan cellulose. A truncated EGPf (EGPfDeltaN30) mutant lacking the proline and hydroxyl-residue rich region at the N terminus was constructed, and its crystal structure was resolved at an atomic resolution of 1.07 A. Our results indicate that the structure of EGPf, which consists of a beta-jelly roll, exhibits structural similarity with the endocellulase of Thermotoga maritima. Additionally, we further determined that the thermostability of EGPf is maintained in part by the binding of Ca(2)(+) in a DxDxDG Ca(2)(+)-binding motif, atypical of most archaeal proteins.
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Atomic resolution of the crystal structure of the hyperthermophilic family 12 endocellulase and stabilizing role of the DxDxDG calcium-binding motif in Pyrococcus furiosus.,Kim HW, Kataoka M, Ishikawa K FEBS Lett. 2012 Apr 5;586(7):1009-13. Epub 2012 Mar 6. PMID:22569255<ref>PMID:22569255</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 3vgi" 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 43587]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ishikawa, K]]
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[[Category: Pyrococcus furiosus]]
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[[Category: Kataoka, M]]
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[[Category: Ishikawa K]]
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[[Category: Kim, H W]]
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[[Category: Kataoka M]]
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[[Category: Beta-jelly roll fold]]
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[[Category: Kim H-W]]
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[[Category: Carbohydrate/sugar binding]]
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[[Category: Hydrolase]]
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Current revision

The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus

PDB ID 3vgi

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