Journal article
The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution
AR Cala, MT Nadeau, J Abendroth, BL Staker, AR Reers, AW Weatherhead, RCJ Dobson, PJ Myler, AO Hudson
Acta Crystallographica Section F Structural Biology Communications | INT UNION CRYSTALLOGRAPHY | Published : 2016
Abstract
In bacteria, the second committed step in the diaminopimelate/lysine anabolic pathways is catalyzed by the enzyme dihydrodipicolinate reductase (DapB). DapB catalyzes the reduction of dihydrodipicolinate to yield tetrahydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of DapB from the human-pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are reported. Protein crystals were grown in conditions consisting of 5%(w/v) PEG 4000, 200 mM sodium acetate, 100 mM sodium citrate tribasic pH 5.5 and were shown to diffract to â2.3 Å resolution. They belonged to space group P4322, with unit-cell parameter..
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Awarded by National Institute of General Medical Sciences
Funding Acknowledgements
The research reported in this publication was supported in part by the National Institute of General Medical Sciences of the National Institutes of Health under award No. R15GM120653 to AOH and RCJD. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. AOH, ARC acknowledges the Thomas H. Gosnell School of Life Sciences at the Rochester Institute of Technology (RIT) for ongoing support of research in the Hudson laboratory. MTN acknowledges the 2016 Summer Undergraduate Research Fellowship in the College of Science at RIT. This project has been funded in part with Federal funds from the National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health, Department of Health and Human Services under contract Nos. HHSN272200700057C and HHSN272201200025C. The Advanced Light Source is supported by the Director, Office of Science, Office of Basic Energy Sciences of the US Department of Energy under contract No. DE-AC02-05CH11231.