View source for 5jqf


==Crystal structure of the lasso peptide Sphingopyxin I (SpI)==
<StructureSection load='5jqf' size='340' side='right'caption='[[5jqf]], [[Resolution|resolution]] 0.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jqf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingopyxis_alaskensis_RB2256 Sphingopyxis alaskensis RB2256]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JQF 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]] 0.85&#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=5jqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqf OCA], [https://pdbe.org/5jqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jqf RCSB], [https://www.ebi.ac.uk/pdbsum/5jqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1D5B387_SPHAL A0A1D5B387_SPHAL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lasso peptides are natural products that assume a unique lariat knot topology. Lasso peptide isopeptidases (IsoPs) eliminate this topology through isopeptide bond cleavage. To probe how these enzymes distinguish between substrates and hydrolyze only isopeptide bonds, we examined the structure and mechanism of a previously uncharacterized IsoP from the proteobacterium Sphingopyxis alaskensis RB2256 (SpI-IsoP). We demonstrate that SpI-IsoP efficiently and specifically linearizes the lasso peptide sphingopyxin I (SpI) and variants thereof. We also present crystal structures of SpI and SpI-IsoP, revealing a threaded topology for the former and a prolyl oligopeptidase (POP)-like fold for the latter. Subsequent structure-guided mutational analysis allowed us to propose roles for active-site residues. Our study sheds light on lasso peptide catabolism and expands the engineering potential of these fascinating molecules.

Structure and Mechanism of the Sphingopyxin I Lasso Peptide Isopeptidase.,Fage CD, Hegemann JD, Nebel AJ, Steinbach RM, Zhu S, Linne U, Harms K, Bange G, Marahiel MA Angew Chem Int Ed Engl. 2016 Oct 4;55(41):12717-21. doi: 10.1002/anie.201605232. , Epub 2016 Sep 9. PMID:27611791<ref>PMID:27611791</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jqf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sphingopyxis alaskensis RB2256]]
[[Category: Bange G]]
[[Category: Fage CD]]
[[Category: Harms K]]
[[Category: Hegemann JD]]
[[Category: Marahiel MA]]