4ypv: Difference between revisions
New page: '''Unreleased structure''' The entry 4ypv is ON HOLD Authors: Pereira, M.R., Maester, C.T., Macedo Lemos, E., Hyvonen, M., Balan, A. Description: High-resolution of an esterase Est8 me... |
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The | ==High-resolution structure of a metagenome-derived esterase Est8== | ||
<StructureSection load='4ypv' size='340' side='right'caption='[[4ypv]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ypv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parvibaculum Parvibaculum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YPV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YPV 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]] 1.85Å</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=4ypv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ypv OCA], [https://pdbe.org/4ypv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ypv RCSB], [https://www.ebi.ac.uk/pdbsum/4ypv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ypv ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Esterases catalyze the cleavage and formation of ester bonds and are members of the diverse family of alpha/beta hydrolase fold. They are useful in industries from different sectors, such as food, detergent, fine chemicals, and biofuel production. In a previous work, 30 positive clones for lipolytic activity were identified from a metagenomic library of a microbial consortium specialized in diesel oil degradation. In this study, a putative gene encoding an esterase/lipase, denominated est8, has been cloned and the corresponding protein expressed recombinantly, purified to homogeneity and characterized functional and structurally. We show that the protein codified by est8 gene, denominated Est8, is an alkaline esterase with high catalytic efficiency against p-nitrophenyl acetate and stable in the presence of up to 10% dimethyl sulfoxide. The three-dimensional structure of Est8 was determined at 1.85-A resolution, allowing the characterization of the substrate-binding pocket and features that rationalize the preference of Est8 for short-chain substrates. In an attempt to increase the size of ligand-binding pocket and enzyme activity against distinct substrates of long chain, we mutated two residues (Met213 and Phe217) that block the substrate channel. A small increase in the reaction velocity for p-nitrophenyl butyrate and p-nitrophenyl valerate hydrolysis was observed. Activity against p-nitrophenyl acetate was reduced. The functional and structural characterization of Est8 is explored in comparison with orthologues. | |||
From a metagenomic source to a high-resolution structure of a novel alkaline esterase.,Pereira MR, Maester TC, Mercaldi GF, de Macedo Lemos EG, Hyvonen M, Balan A Appl Microbiol Biotechnol. 2017 Mar 22. doi: 10.1007/s00253-017-8226-4. PMID:28331945<ref>PMID:28331945</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4ypv" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Macedo Lemos | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Parvibaculum]] | |||
[[Category: Balan A]] | |||
[[Category: Hyvonen M]] | |||
[[Category: Macedo Lemos E]] | |||
[[Category: Maester CT]] | |||
[[Category: Pereira MR]] | |||