2mh1

Enzymatic cyclisation of kalata B1 using sortase A

spinqualitylabelsall models 2mh1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mh1 is a 1 chain structure with sequence from Oldenlandia affinis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KAB1_OLDAF Probably participates in a plant defense mechanism. Has antibiotic activity. Has a diuretic effect. Has a uterotonic effect in humans. Active against the Gram-positive S.aureus with a minimum inhibition concentration of approximately 0.2 microM. Relatively ineffective against Gram-negative bacteria such as E.coli and P.aeruginosa. Inhibitory effect on the growth and development of larvae from H.punctigera. The unmodified form has hemolytic activity, the oxidized form lacks hemolytic activity. If the protein is linearized, hemolytic activity is lost. Publication Abstract from PubMed Disulfide-rich cyclic peptides have generated great interest in the development of peptide-based therapeutics due to their exceptional stability towards chemical, enzymatic or thermal attack. In particular, they have been used as scaffolds onto which bioactive epitopes can be grafted to take advantage of the favorable biophysical properties of disulfide-rich cyclic peptides. To date, the most commonly used method for the head-to-tail cyclization of peptides has been native chemical ligation. In recent years, however, enzyme-mediated cyclization has become a promising new technology due to its efficiency, safety and cost-effectiveness. Sortase A (SrtA) is a bacterial enzyme with transpeptidase activity. It recognizes a C-terminal penta-amino acid motif 'LPXTG' and cleaves the amide bond between Thr and Gly to form a thioacyl-linked intermediate. This intermediate undergoes nucleophilic attack by an N-terminal poly-Gly sequence to form an amide bond between the Thr and N-terminal Gly. Here, we demonstrate that Sortase A can successfully be used to cyclize a variety of small disulfide-rich peptides, including the cyclotide kalata B1, alpha-conotoxin Vc1.1 and sunflower trypsin inhibitor 1 (SFTI-1). These peptides range in size from 14 to 29 amino acids and respectively contain three, two or one disulfide bond within their head-to-tail cyclic backbones. Our findings provide proof-of-concept for the potential broad applicability of enzymatic cyclization of disulfide-rich peptides with therapeutic potential. Semienzymatic Cyclization of Disulfide-rich Peptides Using Sortase A.,Jia X, Kwon S, Wang CI, Huang YH, Chan LY, Tan CC, Rosengren KJ, Mulvenna JP, Schroeder CI, Craik DJ J Biol Chem. 2014 Jan 14. PMID:24425873 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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