View source for 6z68


==A novel metagenomic alpha/beta-fold esterase==
<StructureSection load='6z68' size='340' side='right'caption='[[6z68]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6z68]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_19285 Atcc 19285]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z68 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAMN05443637_118146 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1848 ATCC 19285])</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=6z68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z68 OCA], [https://pdbe.org/6z68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z68 RCSB], [https://www.ebi.ac.uk/pdbsum/6z68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z68 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial lipolytic enzymes of family IV are homologs of the mammalian hormone-sensitive lipases (HSL) and have been successfully used for various biotechnological applications. The broad substrate specificity and ability for enantio-, regio-, and stereoselective hydrolysis are remarkable features of enzymes from this class. Many crystal structures are available for esterases and lipases, but structures of enzyme-substrate or enzyme-inhibitor complexes are less frequent although important to understand the molecular basis of enzyme substrate interaction and to rationalize biochemical enzyme characteristics. Here, we report on the structures of a novel family IV esterase isolated from a metagenomic screen which shows a broad substrate specificity. We solved the crystal structures in the apo form and with a bound substrate analogue at 1.35 A and 1.81 A resolution, respectively. This enzyme named PtEst1 hydrolyzed more than 60 out 96 structurally different ester substrates thus being substrate promiscuous. Its broad substrate specificity is in accord with a large active site cavity, which is covered by an alpha-helical cap domain. The substrate analogue methyl 4-methylumbelliferyl hexylphosphonate was rapidly hydrolyzed by the enzyme leading to a complete inactivation caused by covalent binding of phosphinic acid to the catalytic serine. Interestingly, the alcohol leaving group 4-methylumbelliferone was found remaining in the active site cavity and additionally, a complete inhibitor molecule was found at the cap domain next to the entrance of the substrate tunnel. This unique situation allowed gaining valuable insights into the role of the cap domain for enzyme-substrate interaction of esterases belonging to family IV.

Crystal structures of a novel family IV esterase in free and substrate-bound form.,Hoppner A, Bollinger A, Kobus S, Thies S, Coscolin C, Ferrer M, Jaeger KE, Smits SHJ FEBS J. 2020 Dec 20. doi: 10.1111/febs.15680. PMID:33342083<ref>PMID:33342083</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6z68" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 19285]]
[[Category: Large Structures]]
[[Category: Bollinger, A]]
[[Category: Hoeppner, A]]
[[Category: Jaeger, K E]]
[[Category: Kobus, S]]
[[Category: Smits, S H.J]]
[[Category: Thies, S]]
[[Category: Alpha/beta-fold hydrolase]]
[[Category: Esterase]]
[[Category: Hydrolase]]
[[Category: Inhibitor-bound]]
[[Category: Metagenome]]
[[Category: Substrate promiscuity]]