2ln8 | pdb_00002ln8

The solution structure of theromacin

spinqualitylabelsall models 2ln8, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ln8 is a 1 chain structure with sequence from Hirme. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [THMAC_HIRME] Has a bactericial activity (By similarity). Publication Abstract from PubMed The tertiary structures of theromacin and neuromacin confirmed the macin protein family as a self-contained family of antimicrobial proteins within the superfamily of scorpion toxin-like proteins. The macins, which also comprise hydramacin-1, are antimicrobially active against Gram-positive and Gram-negative bacteria. Despite high sequence identity, the three proteins showed distinct differences with respect to their biological activity. Neuromacin exhibited a significantly stronger capacity to permeabilize the cytoplasmic membrane of Bacillus megaterium than theromacin and hydramacin-1. Accordingly, it is the only macin that displays pore-forming activity and that was potently active against Staphylococcus aureus. Moreover, neuromacin and hydramacin-1 led to an aggregation of bacterial cells that was not observed with theromacin. Analysis of the molecular surface properties of macins allowed confirmation of the barnacle model as the mechanistic model for the aggregation effect. Besides being antimicrobially active, neuromacin and theromacin, in contrast to hydramacin-1, were able to enhance the repair of leech nerves ex vivo. Notably, all three macins enhanced the viability of murine neuroblastoma cells, extending their functional characteristics. As neuromacin appears to be both a functional and structural chimera of hydramacin-1 and theromacin, the putative structural correlate responsible for the nerve repair capacity in leech was located to a cluster of six amino acid residues using the sequence similarity of surface-exposed regions. Macin family of antimicrobial proteins combines antimicrobial and nerve repair activities.,Jung S, Sonnichsen FD, Hung CW, Tholey A, Boidin-Wichlacz C, Haeusgen W, Gelhaus C, Desel C, Podschun R, Waetzig V, Tasiemski A, Leippe M, Grotzinger J J Biol Chem. 2012 Apr 20;287(17):14246-58. Epub 2012 Mar 6. PMID:22396551 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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