| 词条 | Bacteriocin IId |
| 释义 |
| Symbol = Bacteriocin_IId | Name = Bacteriocin_IId | image = PDB 1o82 EBI.jpg | width = | caption = x-ray structure of bacteriocin as-48 at ph 4.5. sulphate bound form | Pfam = PF09221 | Pfam_clan = | InterPro = IPR009086 | SMART = | PROSITE = | MEROPS = | SCOP = 1o82 | TCDB = 1.C.28 | OPM family = | OPM protein = | CAZy = | CDD = }} Bacteriocin AS-48 is a cyclic peptide antibiotic produced by the eubacteria Enterococcus faecalis (Streptococcus faecalis) that shows a broad antimicrobial spectrum against both Gram-positive and Gram-negative bacteria. Bacteriocin AS-48 is encoded by the pheromone-responsive plasmid pMB2, and acts on the plasma membrane in which it opens pores leading to ion leakage and cell death.[1] The globular structure of bacteriocin AS-48 is composed of five alpha helices enclosing a hydrophobic core. The mammalian NK-lysin effector protein of T and natural killer cells has a similar structure, though it lacks sequence homology with bacteriocins AS-48. Bacteriocin uses components of the mannose phosphotransferase system (man-PTS) of susceptible cells as target/receptor. The immunity protein LciA forms a strong complex with the receptor proteins and the bacteriocin, thereby preventing cells from being killed. The complex between LciA and the man-PTS components (IIAB, IIC, and IID) appears to involve an on–off type mechanism that allows complex formation only in the presence of bacteriocin; otherwise no complexes were observed between LciA and the receptor proteins.[2] References1. ^{{cite journal |vauthors=González C, Langdon GM, Bruix M, Gálvez A, Valdivia E, Maqueda M, Rico M | title = Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 21 | pages = 11221–6 |date=October 2000 | pmid = 11005847 | pmc = 17181 | doi = 10.1073/pnas.210301097 | url = }} {{InterPro content|IPR009086}}2. ^{{cite journal|vauthors=Kjos M, Nes IF, Diep DB | title=Mechanisms of resistance to bacteriocins targeting the mannose phosphotransferase system. | journal=Appl Environ Microbiol | year= 2011 | volume= 77 | issue= 10 | pages= 3335–42 | pmid=21421780 | doi=10.1128/AEM.02602-10 | pmc=3126464 }} 1 : Protein domains |
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