2m5z | pdb_00002m5z

Enterocin 7A

spinqualitylabelsall models 2m5z, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2m5z is a 1 chain structure with sequence from Enterococcus faecalis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: FME Related: 2m60 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Leaderless bacteriocins are a class of ribosomally synthesized antimicrobial peptides that are produced by certain Gram-positive bacteria without an N-terminal leader section. These bacteriocins are of great interest due to their potent inhibition of many Gram-positive organisms, including food-borne pathogens such as Listeria and Clostridium spp. We now report the NMR solution structures of enterocins 7A and 7B, leaderless bacteriocins recently isolated from Enterococcus faecalis 710C. These are the first three-dimensional structures to be reported for bacteriocins of this class. Unlike most other linear Gram-positive bacteriocins, enterocins 7A and 7B are highly structured in aqueous conditions. Both peptides are primarily alpha-helical, adopting a similar overall fold. The structures can be divided into three separate alpha-helical regions: the N- and C-termini are both alpha-helical, separated by a central kinked alpha-helix. The overall structures bear an unexpected resemblance to carnocyclin A, a 60-residue peptide that is cyclized via an amide bond between the C- and N-termini and has a saposin fold. Because of synergism observed for other two-peptide leaderless bacteriocins, it was of interest to probe possible binding interactions between enterocins 7A and 7B. However, despite synergistic activity observed between these peptides, no significant binding interaction was observed based on NMR and isothermal calorimetry. Solution Structures of the Linear Leaderless Bacteriocins Enterocin 7A and 7B Resemble Carnocyclin A, a Circular Antimicrobial Peptide.,Lohans CT, Towle KM, Miskolzie M, McKay RT, van Belkum MJ, McMullen LM, Vederas JC Biochemistry. 2013 May 31. PMID:23725536 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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