期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 202, 期 2, 页码 175-181出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2018.01.006
关键词
Cell wall polysaccharide producing enzymes; Co-crystallization of metabolic enzymes; Dehydratase; Protein crystallization; Therapeutic drug target
资金
- San Francisco State University
- National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), U.S. Department of Health and Human Services [HHSN272200700058C, HHSN272201200026C]
Many bacteria require L-rhamnose as a key cell wall component. This sugar is transferred to the cell wall using an activated donor dTDP-L-rhamnose, which is produced by the dTDP-L-rhamnose biosynthetic pathway. We determined the crystal structure of the second enzyme of this pathway dTDP-alpha-D-glucose 4,6-dehydratase (RfbB) from Bacillus anthracis. Interestingly, RfbB only crystallized in the presence of the third enzyme of the pathway RfbC; however, RfbC was not present in the crystal. Our work represents the first complete structural characterization of the four proteins of this pathway in a single Gram-positive bacterium.
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