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NMR structure of an acyl-carrier protein from Borrelia burgdorferi.
Title | NMR structure of an acyl-carrier protein from Borrelia burgdorferi. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Barnwal, RP, Van Voorhis, WC, Varani, G |
Journal | Acta Crystallogr Sect F Struct Biol Cryst Commun |
Volume | 67 |
Issue | Pt 9 |
Pagination | 1137-40 |
Date Published | 2011 Sep 1 |
ISSN | 1744-3091 |
Keywords | Acyl Carrier Protein, Amino Acid Sequence, Bacterial Proteins, Borrelia burgdorferi, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Sequence Alignment, Structural Homology, Protein |
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. |
DOI | 10.1107/S1744309111004386 |
Alternate Journal | Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. |
PubMed ID | 21904063 |