Dommaraju Sudhir, Gorman Michael A, Dogovski Con, Pearce F Grant, Gerrard Juliet A, Dobson Renwick C J, Parker Michael W, Perugini Matthew A
Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville 3010, Victoria, Australia.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):57-60. doi: 10.1107/S1744309109047964. Epub 2009 Dec 25.
Dihydrodipicolinate reductase (DHDPR; EC 1.3.1.26) catalyzes the nucleotide (NADH/NADPH) dependent second step of the lysine-biosynthesis pathway in bacteria and plants. Here, the cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DHDPR from methicillin-resistant Staphylococcus aureus (MRSA-DHDPR) are presented. The enzyme was crystallized in a number of forms, predominantly with ammonium sulfate as a precipitant, with the best crystal form diffracting to beyond 3.65 A resolution. Crystal structures of the apo form as well as of cofactor (NADPH) bound and inhibitor (2,6-pyridinedicarboxylate) bound forms of MRSA-DHDPR will provide insight into the structure and function of this essential enzyme and valid drug target.
二氢二吡啶酸还原酶（DHDPR；EC 1.3.1.26）催化细菌和植物中赖氨酸生物合成途径中依赖核苷酸（NADH/NADPH）的第二步反应。本文介绍了耐甲氧西林金黄色葡萄球菌二氢二吡啶酸还原酶（MRSA-DHDPR）的克隆、表达、纯化、结晶及初步X射线衍射分析。该酶以多种形式结晶，主要以硫酸铵作为沉淀剂，最佳晶体形式的衍射分辨率超过3.65 Å。MRSA-DHDPR的无辅因子形式、结合辅因子（NADPH）形式和结合抑制剂（2,6-吡啶二甲酸）形式的晶体结构将为深入了解这种关键酶的结构和功能以及有效的药物靶点提供帮助。
