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Publication Abstract from PubMed
Nearly complete resonance assignment and the high-resolution NMR structure of the acyl-carrier protein from Borrelia burgdorferi, a target of the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure-determination pipeline, are reported. This protein was chosen as a potential target for drug-discovery efforts because of its involvement in fatty-acid biosynthesis, an essential metabolic pathway, in bacteria. It was possible to assign >98% of backbone resonances and >92% of side-chain resonances using multidimensional NMR spectroscopy. The NMR structure was determined to a backbone r.m.s.d. of 0.4 A and contained four alpha-helices and two 3(10)-helices. A structure-homology search revealed that this protein is highly similar to the acyl-carrier protein from Aquifex aeolicus.
NMR structure of an acyl-carrier protein from Borrelia burgdorferi.,Barnwal RP, Van Voorhis WC, Varani G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1137-40. Epub 2011 Aug 13. PMID:21904063[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Barnwal RP, Van Voorhis WC, Varani G. NMR structure of an acyl-carrier protein from Borrelia burgdorferi. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1137-40. Epub 2011 Aug 13. PMID:21904063 doi:10.1107/S1744309111004386
