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.


3wp3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:46, 20 March 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Xylanase 11C from Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus)==
==Xylanase 11C from Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus)==
-
<StructureSection load='3wp3' size='340' side='right' caption='[[3wp3]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
+
<StructureSection load='3wp3' size='340' side='right'caption='[[3wp3]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3wp3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WP3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WP3 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3wp3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Talaromyces_funiculosus Talaromyces funiculosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WP3 FirstGlance]. <br>
-
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wp3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wp3 RCSB], [http://www.ebi.ac.uk/pdbsum/3wp3 PDBsum]</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=3wp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wp3 OCA], [https://pdbe.org/3wp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wp3 RCSB], [https://www.ebi.ac.uk/pdbsum/3wp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wp3 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/XYNC_TALFU XYNC_TALFU] Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
-
Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus) is one of the mesophilic fungi that can produce high levels of cellulose-related enzymes and are expected to be used for the degradation of polysaccharide biomass. In silico analysis of the genome sequence of T. cellulolyticus detected seven open reading frames (ORFs) showing homology to xylanases from glycoside hydrolase (GH) family 11. The gene encoding the GH11 xylanase C (TcXylC) with the highest activity was used for overproduction and purification of the recombinant enzyme, permitting solving of the crystal structure to a resolution of 1.98 A. In the asymmetric unit, two kinds of the crystal structures of the xylanase were identified. The main structure of the protein showed a beta-jelly roll structure. We hypothesize that one of the two structures represents the open form and the other shows the close form. The changing of the flexible region between the two structures is presumed to induce and accelerate the enzyme reaction. The specificity of xylanase toward the branched xylan is discussed in the context of this structural data and by comparison with the other published structures of xylanases.
+
-
 
+
-
Crystal structure of Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus) GH family 11 xylanase.,Kataoka M, Akita F, Maeno Y, Inoue B, Inoue H, Ishikawa K Appl Biochem Biotechnol. 2014 Oct;174(4):1599-612. doi:, 10.1007/s12010-014-1130-9. Epub 2014 Aug 20. PMID:25138599<ref>PMID:25138599</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: Endo-1,4-beta-xylanase]]
+
[[Category: Large Structures]]
-
[[Category: Inoue, H]]
+
[[Category: Talaromyces funiculosus]]
-
[[Category: Ishikawa, K]]
+
[[Category: Inoue H]]
-
[[Category: Kataoka, M]]
+
[[Category: Ishikawa K]]
-
[[Category: Beta-jelly roll]]
+
[[Category: Kataoka M]]
-
[[Category: Glycoside hydrolase]]
+
-
[[Category: Hydrolase]]
+

Current revision

Xylanase 11C from Talaromyces cellulolyticus (formerly known as Acremonium cellulolyticus)

PDB ID 3wp3

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/3wp3"
Personal tools