Barnwal Ravi P, Van Voorhis Wesley C, Varani G
Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1137-40. doi: 10.1107/S1744309111004386. Epub 2011 Aug 13.
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.
报道了来自伯氏疏螺旋体的酰基载体蛋白几乎完整的共振归属以及高分辨率核磁共振结构，该蛋白是西雅图传染病结构基因组学中心（SSGCID）结构测定流程的一个目标。由于该蛋白参与细菌中脂肪酸生物合成这一重要代谢途径，所以被选为药物研发的潜在靶点。使用多维核磁共振光谱法可归属超过98%的主链共振峰和超过92%的侧链共振峰。核磁共振结构的主链均方根偏差为0.4 Å，包含四个α螺旋和两个3(10)螺旋。结构同源性搜索表明，该蛋白与嗜热栖热菌的酰基载体蛋白高度相似。
