title: NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
abstract: 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 Å and contained four α-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.
authors: Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
authors: Ravi P
authors: RP
authors: Barnwal
authors: Wesley C
authors: WC
authors: Van Voorhis
authors: G
authors: G
authors: Varani
mesh_terms: D000213:Acyl Carrier Protein / Q000737:chemistry*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D025065:Borrelia burgdorferi / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein
chemical_list: D000213:Acyl Carrier Protein; D001426:Bacterial Proteins