3axd: Difference between revisions
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==The truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase V18Y/W203Y in apo-form== | ==The truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase V18Y/W203Y in apo-form== | ||
<StructureSection load='3axd' size='340' side='right' caption='[[3axd]], [[Resolution|resolution]] 1.53Å' scene=''> | <StructureSection load='3axd' size='340' side='right'caption='[[3axd]], [[Resolution|resolution]] 1.53Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3axd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3axd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fibrobacter_succinogenes_subsp._succinogenes_S85 Fibrobacter succinogenes subsp. succinogenes S85]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AXD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53Å</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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3axd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3axd OCA], [https://pdbe.org/3axd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3axd RCSB], [https://www.ebi.ac.uk/pdbsum/3axd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3axd ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GUB_FIBSS GUB_FIBSS] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 17: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3axd" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Glucanase|Glucanase]] | *[[Glucanase 3D structures|Glucanase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Fibrobacter succinogenes subsp. succinogenes | [[Category: Fibrobacter succinogenes subsp. succinogenes S85]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chen | [[Category: Chen CC]] | ||
[[Category: Cheng | [[Category: Cheng YS]] | ||
[[Category: Guo | [[Category: Guo RT]] | ||
[[Category: Huang | [[Category: Huang CH]] | ||
[[Category: Huang | [[Category: Huang JW]] | ||
[[Category: Ko | [[Category: Ko TP]] | ||
[[Category: Lai | [[Category: Lai HL]] | ||
[[Category: Lin | [[Category: Lin CY]] | ||
[[Category: Liu | [[Category: Liu JR]] | ||
[[Category: Ma | [[Category: Ma Y]] | ||
[[Category: Zheng | [[Category: Zheng Y]] | ||
Latest revision as of 11:48, 11 October 2023
The truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase V18Y/W203Y in apo-formThe truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase V18Y/W203Y in apo-form
Structural highlights
FunctionPublication Abstract from PubMed1,3-1,4-beta-D: -Glucanase has been widely used as a feed additive to help non-ruminant animals digest plant fibers, with potential in increasing nutrition turnover rate and reducing sanitary problems. Engineering of enzymes for better thermostability is of great importance because it not only can broaden their industrial applications, but also facilitate exploring the mechanism of enzyme stability from structural point of view. To obtain enzyme with higher thermostability and specific activity, structure-based rational design was carried out in this study. Eleven mutants of Fibrobacter succinogenes 1,3-1,4-beta-D: -glucanase were constructed in attempt to improve the enzyme properties. In particular, the crude proteins expressed in Pichia pastoris were examined firstly to ensure that the protein productions meet the need for industrial fermentation. The crude protein of V18Y mutant showed a 2 degrees C increment of Tm and W203Y showed approximately 30% increment of the specific activity. To further investigate the structure-function relationship, some mutants were expressed and purified from P. pastoris and Escherichia coli. Notably, the specific activity of purified W203Y which was expressed in E. coli was 63% higher than the wild-type protein. The double mutant V18Y/W203Y showed the same increments of Tm and specific activity as the single mutants did. When expressed and purified from E. coli, V18Y/W203Y showed similar pattern of thermostability increment and 75% higher specific activity. Furthermore, the apo-form and substrate complex structures of V18Y/W203Y were solved by X-ray crystallography. Analyzing protein structure of V18Y/W203Y helps elucidate how the mutations could enhance the protein stability and enzyme activity. Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-beta-D: -glucanase.,Huang JW, Cheng YS, Ko TP, Lin CY, Lai HL, Chen CC, Ma Y, Zheng Y, Huang CH, Zou P, Liu JR, Guo RT Appl Microbiol Biotechnol. 2011 Sep 30. PMID:21959377[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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