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| | <StructureSection load='5hup' size='340' side='right'caption='[[5hup]], [[Resolution|resolution]] 3.42Å' scene=''> | | <StructureSection load='5hup' size='340' side='right'caption='[[5hup]], [[Resolution|resolution]] 3.42Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hup]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HUP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hup]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_MGAS10750 Streptococcus pyogenes MGAS10750]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HUP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.42Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hul|5hul]], [[5huo|5huo]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinate-nucleotide_diphosphorylase_(carboxylating) Nicotinate-nucleotide diphosphorylase (carboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.19 2.4.2.19] </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=5hup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hup OCA], [https://pdbe.org/5hup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hup RCSB], [https://www.ebi.ac.uk/pdbsum/5hup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hup ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hup OCA], [http://pdbe.org/5hup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hup RCSB], [http://www.ebi.ac.uk/pdbsum/5hup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hup ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q1J647_STRPF Q1J647_STRPF] |
| | <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: Booth, W T]] | + | [[Category: Streptococcus pyogenes MGAS10750]] |
| - | [[Category: Chruszcz, M]] | + | [[Category: Booth WT]] |
| - | [[Category: Quinolinate phosphoribosyltransferase]] | + | [[Category: Chruszcz M]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q1J647_STRPF
Publication Abstract from PubMed
Streptococcus pyogenes, also known as Group A Strep (GAS), is an obligate human pathogen that is responsible for millions of infections and numerous deaths per year. Infection manifestations can range from simple, acute pharyngitis to more complex, necrotizing fasciitis. To date, most treatments for GAS infections involve the use of common antibiotics including tetracycline and clindamycin. Unfortunately, new strains have been identified that are resistant to these drugs, therefore, new targets must be identified to treat drug-resistant strains. This work is focused on the structural and functional characterization of three proteins: spNadC, spNadD, and spNadE. These enzymes are involved in the biosynthesis of nicotinamide adenine dinucleotide (NAD+ ). The structures of spNadC and spNadE were determined. SpNadC is suggested to play a role in GAS virulence, while spNadE, functions as an NAD synthetase and is considered to be a new drug target. Determination of the spNadE structure uncovered a putative, NH3 channel, which may provide insight into the mechanistic details of NH3 -dependent NAD+ synthetases in prokaryotes. ENZYMES: Quinolinate phosphoribosyltransferase: EC2.4.2.19 and NAD synthetase: EC6.3.1.5. DATABASE: Protein structures for spNadC, spNadCDelta69A , and spNadE are deposited into Protein Data Bank under the accession codes 5HUL, 5HUO & 5HUP, and 5HUH & 5HUJ, respectively.
Streptococcus pyogenes quinolinate-salvage pathway-structural and functional studies of quinolinate phosphoribosyl transferase and NH3 -dependent NAD+ synthetase.,Booth WT, Morris TL, Mysona DP, Shah MJ, Taylor LK, Karlin TW, Clary K, Majorek KA, Offermann LR, Chruszcz M FEBS J. 2017 Aug;284(15):2425-2441. doi: 10.1111/febs.14136. Epub 2017 Jul 7. PMID:28618168[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Booth WT, Morris TL, Mysona DP, Shah MJ, Taylor LK, Karlin TW, Clary K, Majorek KA, Offermann LR, Chruszcz M. Streptococcus pyogenes quinolinate-salvage pathway-structural and functional studies of quinolinate phosphoribosyl transferase and NH3 -dependent NAD+ synthetase. FEBS J. 2017 Aug;284(15):2425-2441. doi: 10.1111/febs.14136. Epub 2017 Jul 7. PMID:28618168 doi:http://dx.doi.org/10.1111/febs.14136
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