4ecm
From Proteopedia
(Difference between revisions)
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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=4ecm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ecm OCA], [http://pdbe.org/4ecm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ecm RCSB], [http://www.ebi.ac.uk/pdbsum/4ecm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ecm 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=4ecm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ecm OCA], [http://pdbe.org/4ecm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ecm RCSB], [http://www.ebi.ac.uk/pdbsum/4ecm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ecm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | L-Rhamnose is a ubiquitous bacterial cell-wall component. The biosynthetic pathway for its precursor dTDP-L-rhamnose is not present in humans, which makes the enzymes of the pathway potential drug targets. In this study, the three-dimensional structure of the first protein of this pathway, glucose-1-phosphate thymidylyltransferase (RfbA), from Bacillus anthracis was determined. In other organisms this enzyme is referred to as RmlA. RfbA was co-crystallized with the products of the enzymatic reaction, dTDP-alpha-D-glucose and pyrophosphate, and its structure was determined at 2.3 A resolution. This is the first reported thymidylyltransferase structure from a Gram-positive bacterium. RfbA shares overall structural characteristics with known RmlA homologs. However, RfbA exhibits a shorter sequence at its C-terminus, which results in the absence of three alpha-helices involved in allosteric site formation. Consequently, RfbA was observed to exhibit a quaternary structure that is unique among currently reported glucose-1-phosphate thymidylyltransferase bacterial homologs. These structural analyses suggest that RfbA may not be allosterically regulated in some organisms and is structurally distinct from other RmlA homologs. | ||
| - | + | Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme glucose-1-phosphate thymidylyltransferase (RfbA).,Baumgartner J, Lee J, Halavaty AS, Minasov G, Anderson WF, Kuhn ML Acta Crystallogr F Struct Biol Commun. 2017 Nov 1;73(Pt 11):621-628. doi:, 10.1107/S2053230X17015357. Epub 2017 Oct 30. PMID:29095156<ref>PMID:29095156</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4ecm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Shuvalova, L]] | [[Category: Shuvalova, L]] | ||
[[Category: Winsor, J]] | [[Category: Winsor, J]] | ||
| + | [[Category: Csgid]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 08:01, 15 November 2017
2.3 Angstrom Crystal Structure of a Glucose-1-phosphate Thymidylyltransferase from Bacillus anthracis in Complex with Thymidine-5-diphospho-alpha-D-glucose and Pyrophosphate
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