5jrl | pdb_00005jrl

Crystal Structure of the Sphingopyxin I Lasso Peptide Isopeptidase SpI-IsoP (Native)

spinqualitylabelsall models 5jrl, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jrl is a 4 chain structure with sequence from Sphingopyxis alaskensis RB2256. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1GQ33_SPHAL 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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