Structural highlights
Publication Abstract from PubMedThe protein AlbG is a self-resistance factor against albicidin, a nonribosomally encoded hybrid polyketide-peptide with antibiotic and phytotoxic properties produced by Xanthomonas albilineans. Primary-sequence analysis indicates that AlbG is a member of the pentapeptide-repeat family of proteins (PRP). The structure of AlbG from X. albilineans was determined at 2.0 A resolution by SAD phasing using data collected from a single trimethyllead acetate derivative on a home source. AlbG folds into a right-handed quadrilateral beta-helix composed of approximately eight semi-regular coils. The regularity of the beta-helix is blemished by a large loop/deviation in the beta-helix between coils 4 and 5. The C-terminus of the beta-helix is capped by a dimerization module, yielding a dimer with a 110 A semi-collinear beta-helical axis. This method of dimer formation appears to be common to all PRP proteins that confer resistance to topoisomerase poisons and contrasts with most PRP proteins, which are typically monomeric. Pentapeptide-repeat proteins that act as topoisomerase poison resistance factors have a common dimer interface.,Vetting MW, Hegde SS, Zhang Y, Blanchard JS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Mar 1;67(Pt, 3):296-302. Epub 2011 Feb 18. PMID:21393830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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