View source for 4wy8


==Structural analysis of two fungal esterases from Rhizomucor miehei explaining their substrate specificity==
<StructureSection load='4wy8' size='340' side='right'caption='[[4wy8]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4wy8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizomucor_miehei_CAU432 Rhizomucor miehei CAU432]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WY8 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]] 2.27&#8491;</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=4wy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wy8 OCA], [https://pdbe.org/4wy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wy8 RCSB], [https://www.ebi.ac.uk/pdbsum/4wy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wy8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0M3KKZ9_RHIMI A0A0M3KKZ9_RHIMI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two hormone-sensitive lipase (HSL) family esterases (RmEstA and RmEstB) from the thermophilic fungus Rhizomucor miehei, exhibiting distinct substrate specificity, have been recently reported to show great potential in industrial applications. In this study, the crystal structures of RmEstA and RmEstB were determined at 2.15 A and 2.43 A resolutions, respectively. The structures of RmEstA and RmEstB showed two distinctive domains--a catalytic domain and a cap domain--with the classical Alpha/Beta-hydrolase fold. Catalytic triads consisting of residues Ser161, Asp262 and His292 in RmEstA, and Ser164, Asp261 and His291 in RmEstB were found in the respective canonical positions. Structural comparison of RmEstA and RmEstB revealed that their distinct substrate specificity might be attributed to their different substrate-binding pockets. The aromatic amino acids Phe222 and Trp92, located in the center of the substrate-binding pocket of RmEstB, blocked this pocket, thus narrowing its catalytic range for substrates (C2--C8). Two mutants (F222A and W92F in RmEstB) showing higher catalytic activity toward long-chain substrates further confirmed the hypothesized interference. This is the first report of HSL family esterase structures from filamentous fungi. The information on structure-function relationships could open important avenues of exploration for further industrial applications of esterases.

Structural insights into the substrate specificity of two esterases from the thermophilic Rhizomucor miehei.,Yang S, Qin Z, Duan X, Yan Q, Jiang Z J Lipid Res. 2015 Jun 23. pii: jlr.M060673. PMID:26108223<ref>PMID:26108223</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wy8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizomucor miehei CAU432]]
[[Category: Duan X]]
[[Category: Jiang Z]]
[[Category: Qin Z]]
[[Category: Yan Q]]
[[Category: Yang S]]