View source for 4oyy


==Humicola insolens cutinase==
<StructureSection load='4oyy' size='340' side='right'caption='[[4oyy]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4oyy]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OYY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OYY 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]] 3&#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=4oyy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oyy OCA], [https://pdbe.org/4oyy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oyy RCSB], [https://www.ebi.ac.uk/pdbsum/4oyy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oyy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A075B5G4_HUMIN A0A075B5G4_HUMIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The interaction of lipolytic enzymes with anionic surfactants is of great interest with respect to industrially produced detergents. Here, we report the interaction of cutinase from the thermophilic fungus Humicola insolens with the anionic surfactant SDS, and show the enzyme specifically binds a single SDS molecule under nondenaturing concentrations. Protein interaction with SDS was investigated by NMR, ITC and molecular dynamics simulations. The NMR resonances of the protein were assigned, with large stretches of the protein molecule not showing any detectable resonances. SDS is shown to specifically interact with the loops surrounding the catalytic triad with medium affinity (Ka approximately 105 M-1 ). The mode of binding is closely similar to that seen previously for binding of amphiphilic molecules and substrate analogues to cutinases, and hence SDS acts as a substrate mimic. In addition, the structure of the enzyme has been solved by X-ray crystallography in its apo form and after cocrystallization with diethyl p-nitrophenyl phosphate (DNPP) leading to a complex with monoethylphosphate (MEP) esterified to the catalytically active serine. The enzyme has the same fold as reported for other cutinases but, unexpectedly, esterification of the active site serine is accompanied by the ethylation of the active site histidine which flips out from its usual position in the triad.

Thermodynamic and structural investigation of the specific SDS binding of humicola insolens cutinase.,Kold D, Dauter Z, Laustsen AK, Brzozowski AM, Turkenburg JP, Nielsen AD, Koldso H, Petersen E, Schiott B, De Maria L, Wilson KS, Svendsen A, Wimmer R Protein Sci. 2014 May 16. doi: 10.1002/pro.2489. PMID:24832484<ref>PMID:24832484</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4oyy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cutinase 3D structures|Cutinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Humicola insolens]]
[[Category: Large Structures]]
[[Category: Brzozowski AM]]
[[Category: Dauter ZD]]
[[Category: Turkenburg JP]]
[[Category: Wilson KS]]