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| | ==Crystal Structure of NadC Deletion Mutant in Cubic Space Group== | | ==Crystal Structure of NadC Deletion Mutant in Cubic Space Group== |
| - | <StructureSection load='5hul' size='340' side='right' caption='[[5hul]], [[Resolution|resolution]] 2.85Å' scene=''> | + | <StructureSection load='5hul' size='340' side='right'caption='[[5hul]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hul]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HUL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hul]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_NZ131 Streptococcus pyogenes NZ131]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HUL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.855Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5huh|5huh]], [[5huj|5huj]], [[5huo|5huo]], [[5hup|5hup]]</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=5hul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hul OCA], [https://pdbe.org/5hul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hul RCSB], [https://www.ebi.ac.uk/pdbsum/5hul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hul ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hul OCA], [http://pdbe.org/5hul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hul RCSB], [http://www.ebi.ac.uk/pdbsum/5hul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hul ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H3BVM1_STRPZ A0A0H3BVM1_STRPZ] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5hul" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5hul" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Booth, W T]] | + | [[Category: Large Structures]] |
| - | [[Category: Chruszcz, M]] | + | [[Category: Streptococcus pyogenes NZ131]] |
| - | [[Category: Quinolinate phosphoribosyltransferase]] | + | [[Category: Booth WT]] |
| - | [[Category: Transferase]] | + | [[Category: Chruszcz M]] |
| Structural highlights
Function
A0A0H3BVM1_STRPZ
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.
See Also
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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