View source for 5wsl


==Structural studies of keratinase from Meiothermus taiwanensis WR-220==
<StructureSection load='5wsl' size='340' side='right'caption='[[5wsl]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wsl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Meiothermus_taiwanensis_WR-220 Meiothermus taiwanensis WR-220]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WSL FirstGlance]. <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]] 1.5&#8491;</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=SO4:SULFATE+ION'>SO4</scene></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=5wsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wsl OCA], [https://pdbe.org/5wsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wsl RCSB], [https://www.ebi.ac.uk/pdbsum/5wsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wsl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2H4A2Y5_9DEIN A0A2H4A2Y5_9DEIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Billions of tons of keratin bio-wastes are generated by poultry industry annually but discarded that result in serious environmental pollution. Keratinase is a broad spectrum protease with the unique ability to degrade keratin, providing an eco-friendly way to convert keratin wastes to valuable amino acids. In this report, a feather-degrading thermophilic bacterium, Meiothermus taiwanensis WR-220, was investigated due to its ability to apparently complete feather decay at 65 degrees C in two days. By genomics, proteomics, and biochemical approaches, the extracellular heat-stable keratinase (MtaKer) from M. taiwanensis WR-220 was identified. The recombinant MtaKer (rMtaKer) possesses keratinolytic activities at temperatures ranging from 25 to 75 degrees C and pH from 4 to 11, with a maximum keratinolytic activity at 65 degrees C and pH 10. The phylogenetic and structural analysis revealed that MtaKer shares low sequence identity but high structural similarity with known keratinases. Accordingly, our findings have enabled the discovery of more keratinases from other extremophiles, Thermus and Deinococcus. Proteins encoded in the extremophiles shall be evolved to be functional in the extreme conditions. Hence, our study expands the current boundary of hunting keratinases that can tolerate extreme conditions for keratin wastes biorecycle and other industrial applications.

The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles.,Wu WL, Chen MY, Tu IF, Lin YC, EswarKumar N, Chen MY, Ho MC, Wu SH Sci Rep. 2017 Jul 5;7(1):4658. doi: 10.1038/s41598-017-04723-4. PMID:28680127<ref>PMID:28680127</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wsl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Meiothermus taiwanensis WR-220]]
[[Category: Chen MY]]
[[Category: Ho MC]]
[[Category: Tu IF]]
[[Category: Wu SH]]