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| | <StructureSection load='6xhk' size='340' side='right'caption='[[6xhk]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='6xhk' size='340' side='right'caption='[[6xhk]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6xhk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XHK FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XHK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.405 1.1.1.405] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6xhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xhk OCA], [https://pdbe.org/6xhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xhk RCSB], [https://www.ebi.ac.uk/pdbsum/6xhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xhk ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6xhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xhk OCA], [https://pdbe.org/6xhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xhk RCSB], [https://www.ebi.ac.uk/pdbsum/6xhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xhk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Function == | |
| - | [[https://www.uniprot.org/uniprot/TARJ1_STAA8 TARJ1_STAA8]] Catalyzes the NADPH dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate.[HAMAP-Rule:MF_02069]<ref>PMID:15362865</ref> | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Li FKK]] |
| - | [[Category: Li, F K.K]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Strynadka, N C.J]] | + | |
| - | [[Category: Alcohol dehydrogenase]]
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| Structural highlights
Publication Abstract from PubMed
The cell wall of many pathogenic Gram-positive bacteria contains ribitol-phosphate wall teichoic acid (WTA), a polymer that is linked to virulence and regulation of essential physiological processes including cell division. CDP-ribitol, the activated precursor for ribitol-phosphate polymerization, is synthesized by a cytidylyltransferase and reductase pair known as TarI and TarJ, respectively. In this study, we present crystal structures of Staphylococcus aureus TarI and TarJ in their apo forms and in complex with substrates and products. The TarI structures illustrate the mechanism of CDP-ribitol synthesis from CTP and ribitol-phosphate and reveal structural changes required for substrate binding and catalysis. Insights into the upstream step of ribulose-phosphate reduction to ribitol-phosphate is provided by the structures of TarJ. Furthermore, we propose a general topology of the enzymes in a heterotetrameric form built using restraints from crosslinking mass spectrometry analysis. Together, our data present molecular details of CDP-ribitol production that may aid in the design of inhibitors against WTA biosynthesis.
Crystallographic analysis of TarI and TarJ, a cytidylyltransferase and reductase pair for CDP-ribitol synthesis in Staphylococcus aureus wall teichoic acid biogenesis.,Li FKK, Gale RT, Petrotchenko EV, Borchers CH, Brown ED, Strynadka NCJ J Struct Biol. 2021 Apr 2:107733. doi: 10.1016/j.jsb.2021.107733. PMID:33819634[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li FKK, Gale RT, Petrotchenko EV, Borchers CH, Brown ED, Strynadka NCJ. Crystallographic analysis of TarI and TarJ, a cytidylyltransferase and reductase pair for CDP-ribitol synthesis in Staphylococcus aureus wall teichoic acid biogenesis. J Struct Biol. 2021 Apr 2:107733. doi: 10.1016/j.jsb.2021.107733. PMID:33819634 doi:http://dx.doi.org/10.1016/j.jsb.2021.107733
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