View source for 6qpr


==Rhizomucor miehei lipase propeptide complex, Ser95/Ile96 deletion mutant==
<StructureSection load='6qpr' size='340' side='right'caption='[[6qpr]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qpr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizomucor_miehei Rhizomucor miehei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QPR 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=6qpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qpr OCA], [https://pdbe.org/6qpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qpr RCSB], [https://www.ebi.ac.uk/pdbsum/6qpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qpr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIP_RHIMI LIP_RHIMI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many proteins are synthesized as precursors, with propeptides playing a variety of roles such as assisting in folding or preventing them from being active within the cell. While the precise role of the propeptide in fungal lipases is not completely understood, it was previously reported that mutations in the propeptide region of the Rhizomucor miehei lipase have an influence on the activity of the mature enzyme, stressing the importance of the amino acid composition of this region. We here report two structures of this enzyme in complex with its propeptide, which suggests that the latter plays a role in the correct maturation of the enzyme. Most importantly, we demonstrate that the propeptide shows inhibition of lipase activity in standard lipase assays and propose that an important role of the propeptide is to ensure that the enzyme is not active during its expression pathway in the original host.

Novel Inhibitory Function of the Rhizomucor miehei Lipase Propeptide and Three-Dimensional Structures of Its Complexes with the Enzyme.,Moroz OV, Blagova E, Reiser V, Saikia R, Dalal S, Jorgensen CI, Bhatia VK, Baunsgaard L, Andersen B, Svendsen A, Wilson KS ACS Omega. 2019 Jun 7;4(6):9964-9975. doi: 10.1021/acsomega.9b00612. eCollection , 2019 Jun 30. PMID:31460089<ref>PMID:31460089</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qpr" style="background-color:#fffaf0;"></div>

==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhizomucor miehei]]
[[Category: Andersen B]]
[[Category: Baunsgaard L]]
[[Category: Blagova E]]
[[Category: Dalal S]]
[[Category: Jorgensen CI]]
[[Category: Moroz OV]]
[[Category: Reiser V]]
[[Category: Saikia R]]
[[Category: Svendsen A]]
[[Category: Wilson KS]]