2bl8
From Proteopedia
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1.6 ANGSTROM CRYSTAL STRUCTURE OF ENTA-IM: A BACTERIAL IMMUNITY PROTEIN CONFERRING IMMUNITY TO THE ANTIMICROBIAL ACTIVITY OF THE PEDIOCIN-LIKE BACTERIOCIN, ENTEROCIN A
Overview
Many Gram-positive bacteria produce ribosomally synthesized antimicrobial, peptides, often termed bacteriocins. Genes encoding pediocin-like, bacteriocins are generally cotranscribed with or in close vicinity to a, gene encoding a cognate immunity protein that protects the, bacteriocin-producer from their own bacteriocin. We present the first, crystal structure of a pediocin-like immunity protein, EntA-im, conferring, immunity to the bacteriocin enterocin A. Determination of the structure of, this 103-amino acid protein revealed that it folds into an antiparallel, four-helix bundle with a flexible C-terminal part. The fact that the, immunity protein conferring immunity to carnobacteriocin B2 also consists, of a four-helix bundle (Sprules, T., Kawulka, K. E., and Vederas, J. C., (2004) ... [(full description)]
About this Structure
2BL8 is a [Single protein] structure of sequence from [Enterococcus faecium] with FLC as [ligand]. Full crystallographic information is available from [OCA].
Reference
1.6-Angstroms crystal structure of EntA-im. A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A., Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J, J Biol Chem. 2005 May 13;280(19):19045-50. Epub 2005 Mar 7. PMID:15753083
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