crystal, solution and in silico structural studies of dihydrodipicolinate synthase from the common grapevine水晶,解决方案和硅结构研究dihydrodipicolinate合成酶的常见的小道消息.pdfVIP

Crystal, Solution and In silico Structural Studies of Dihydrodipicolinate Synthase from the Common Grapevine 1,2 1,2 3 4 5,6 Sarah C. Atkinson , Con Dogovski , Matthew T. Downton , F. Grant Pearce , Cyril F. Reboul , 5 4 2,4 3 1,2 Ashley M. Buckle , Juliet A. Gerrard , Renwick C. J. Dobson , John Wagner , Matthew A. Perugini * 1 Department of Biochemistry, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia, 2 Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Victoria, Australia, 3 IBM Research Collaboratory for Life Sciences-Melbourne, Victorian Life Sciences Computation Initiative, Carlton, Australia, 4 Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch, New Zealand, 5 Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia, 6 ARC Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, Victoria, Australia Abstract Dihydrodipicolinate synthase (DHDPS) catalyzes the rate limiting step in lysine biosynthesis in bacteria and plants. The structure of DHDPS has been determined from several bacterial species and shown in most cases to form a homotetramer or dimer of dimers. However, only one plant DHDPS structure has been determined to date from the wild tobacco species, Nicotiana sylvestr