5ol1

Crystal structure of an inactivated Ssp SICLOPPS intein with a CAFHPQ extein

spinqualitylabelsall models 5ol1, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ol1 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BME, EDO, PGE, SO4 NonStd Res: CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Inteins carry out protein-splicing reactions, which are utilised in protein chemistry, protein engineering and biotechnological applications. Rearrangement of the order of the domains in split-inteins results in a head-to-tail cyclisation of the target sequence, which can be used to genetically encode and express libraries of cyclic peptides. The efficiency of the splicing reaction depends on the target sequence. Here we used mass spectrometry to assess the cyclic peptide formation of different, hexameric target sequences in vivo by the DnaE split-inteins from Synechocystis sp. and Nostoc punctiforme, revealing a strong impact by the target sequence and intein on the intracellular peptide concentration. Furthermore, we determined the crystal structures of their pre-splicing complexes, which allowed us to identify F-Block Asp17 as crucial for the DnaE-mediated splicing reaction. Mechanistic insights into cyclic peptide generation by DnaE split-inteins through quantitative and structural investigation.,Kick L, Harteis S, Koch MF, Schneider S Chembiochem. 2017 Sep 15. doi: 10.1002/cbic.201700503. PMID:28914478 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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