This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3vgi

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:39, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus==
==The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus==
-
<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 ==
-
<table><tr><td colspan='2'>[[3vgi]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VGI FirstGlance]. <br>
+
<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>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><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]] 1.07&#8491;</td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3az0|3az0]]</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>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eglA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])</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>
-
<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=3vgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vgi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vgi RCSB], [http://www.ebi.ac.uk/pdbsum/3vgi PDBsum]</span></td></tr>
+
</table>
-
<table>
+
== Function ==
-
<div style="background-color:#fffaf0;">
+
[https://www.uniprot.org/uniprot/Q9V2T0_9EURY Q9V2T0_9EURY]
-
== Publication Abstract from PubMed ==
+
-
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.
+
-
 
+
-
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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
-
[[Category: Ishikawa, K.]]
+
[[Category: Ishikawa K]]
-
[[Category: Kataoka, M.]]
+
[[Category: Kataoka M]]
-
[[Category: Kim, H W.]]
+
[[Category: Kim H-W]]
-
[[Category: Beta-jelly roll fold]]
+
-
[[Category: Carbohydrate/sugar binding]]
+
-
[[Category: Hydrolase]]
+

Current revision

The crystal structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus

PDB ID 3vgi

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3vgi"
Personal tools