Journal article
Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1 angstrom resolution
Kubra F Naqvi, Bart L Staker, Renwick CJ Dobson, Dmitry Serbzhinskiy, Banumathi Sankaran, Peter J Myler, Andre O Hudson
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | INT UNION CRYSTALLOGRAPHY | Published : 2016
Abstract
The enzyme dihydrodipicolinate synthase catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis. Dihydrodipicolinate synthase catalyzes the condensation of L-aspartate 4-semialdehyde and pyruvate to synthesize L-2,3-dihydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are presented. Protein crystals were grown in conditions consisting of 20%(w/v) PEG 4000, 100 mM sodium citrate tribasic pH 5.5 and were shown to diffract to ∼2.10 Å reso..
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Awarded by Federal funds from the National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Department of Health and Human Services (HHS)
Awarded by Office of Science, Office of Basic Energy Sciences of the US Department of Energy (DOE)
Funding Acknowledgements
AOH and KFN acknowledge the Thomas H. Gosnell School of Life Sciences for ongoing support of research in the Hudson laboratory. AOH acknowledges the College of Science Dean's Research Initiation Grant (D-RIG) Program at the Rochester Institute of Technology for support of this work. This project has been funded in part with Federal funds from the National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Department of Health and Human Services (HHS) under Contract Nos. HHSN272200700057C and HHSN272201200025C. The Berkeley Center for Structural Biology is supported in part by the NIH, National Institute of General Medical Sciences (NIGMS) and the Howard Hughes Medical Institute (HHMI). The Advanced Light Source is supported by the Director, Office of Science, Office of Basic Energy Sciences of the US Department of Energy (DOE) under Contract No. DE-AC02-05CH11231.