3sc6
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sc6 OCA], [http://pdbe.org/3sc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sc6 RCSB], [http://www.ebi.ac.uk/pdbsum/3sc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sc6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sc6 OCA], [http://pdbe.org/3sc6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sc6 RCSB], [http://www.ebi.ac.uk/pdbsum/3sc6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sc6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacillus anthracis is the causative agent of the deadly disease Anthrax. Its use in bioterrorism and its ability to re-emerge have brought renewed interest in this organism. B. anthracis is a Gram-positive bacterium that adds L-rhamnose to its cell-wall polysaccharides using the activated donor dTDP-beta-L-rhamnose. The enzymes involved in the biosynthesis of the activated donor are absent in humans, which make them ideal targets for therapeutic development to combat pathogens. Here, the 2.65 A resolution crystal structure of the fourth enzyme in the dTDP-beta-L-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro-beta-L-rhamnose reductase (RfbD), is presented in complex with NADP(+). This enzyme catalyzes the reduction of dTDP-4-dehydro-beta-L-rhamnose to dTDP-beta-L-rhamnose. Although the protein was co-crystallized in the presence of Mg(2+), the protein lacks the conserved residues that coordinate Mg(2+). | ||
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| + | Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD).,Law A, Stergioulis A, Halavaty AS, Minasov G, Anderson WF, Kuhn ML Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):644-650. doi:, 10.1107/S2053230X17015746. Epub 2017 Nov 6. PMID:29199984<ref>PMID:29199984</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3sc6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:19, 13 December 2017
2.65 Angstrom resolution crystal structure of dTDP-4-dehydrorhamnose reductase (rfbD) from Bacillus anthracis str. Ames in complex with NADP
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Categories: DTDP-4-dehydrorhamnose reductase | Anderson, W F | Structural genomic | Halavaty, A S | Kuhn, M | Minasov, G | Peterson, S | Shuvalova, L | Bacillus anthracis str. ame | Catalyzes formation of dtdp-4-dehydro-6-deoxy-l-mannose | Csgid | Dtdp-4-dehydrorhamnose reductase | Infectious disease | Nadph and h+ from dtdp-6-deoxy-l-mannose and nadp+ | Oxidoreductase | Rfbd | Rhamnose biosynthetic pathway | Rossmann fold
