<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Gokey T</submitter><funding>National Institute of Allergy and Infectious Diseases</funding><funding>San Francisco State University</funding><funding>U.S. Department of Health and Human Services</funding><funding>NIAID NIH HHS</funding><funding>National Institutes of Health</funding><pagination>175-181</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5864537</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>202(2)</volume><pubmed_abstract>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-α-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.</pubmed_abstract><journal>Journal of structural biology</journal><pubmed_title>Structure of the Bacillus anthracis dTDP-l-rhamnose biosynthetic pathway enzyme: dTDP-α-d-glucose 4,6-dehydratase, RfbB.</pubmed_title><pmcid>PMC5864537</pmcid><funding_grant_id>HHSN272201200026C</funding_grant_id><funding_grant_id>HHSN272200700058C</funding_grant_id><pubmed_authors>Halavaty AS</pubmed_authors><pubmed_authors>Anderson WF</pubmed_authors><pubmed_authors>Kuhn ML</pubmed_authors><pubmed_authors>Gokey T</pubmed_authors><pubmed_authors>Minasov G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure of the Bacillus anthracis dTDP-l-rhamnose biosynthetic pathway enzyme: dTDP-α-d-glucose 4,6-dehydratase, RfbB.</name><description>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-α-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.</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 May</publication><modification>2024-11-19T19:00:00.885Z</modification><creation>2019-06-06T22:47:56Z</creation></dates><accession>S-EPMC5864537</accession><cross_references><pubmed>29331609</pubmed><doi>10.1016/j.jsb.2018.01.006</doi></cross_references></HashMap>