7pkj
From Proteopedia
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==Streptococcus pyogenes apo GapN== | ==Streptococcus pyogenes apo GapN== | ||
| - | <StructureSection load='7pkj' size='340' side='right'caption='[[7pkj]]' scene=''> | + | <StructureSection load='7pkj' size='340' side='right'caption='[[7pkj]], [[Resolution|resolution]] 1.99Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PKJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7pkj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_M49_591 Streptococcus pyogenes M49 591]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PKJ FirstGlance]. <br> |
| - | </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=7pkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pkj OCA], [https://pdbe.org/7pkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pkj RCSB], [https://www.ebi.ac.uk/pdbsum/7pkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pkj ProSAT]</span></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]] 1.989Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=7pkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pkj OCA], [https://pdbe.org/7pkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pkj RCSB], [https://www.ebi.ac.uk/pdbsum/7pkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pkj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q99Z67_STRP1 Q99Z67_STRP1] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The strict human pathogen Streptococcus pyogenes causes infections of varying severity, ranging from self-limiting suppurative infections to life-threatening diseases like necrotizing fasciitis or streptococcal toxic shock syndrome. Here, we show that the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase GapN is an essential enzyme for S. pyogenes. GapN converts glyceraldehyde 3-phosphate into 3-phosphoglycerate coupled to the reduction of NADP to NADPH. The knock-down of gapN by antisense peptide nucleic acids (asPNA) significantly reduces viable bacterial counts of S. pyogenes laboratory and macrolide-resistant clinical strains in vitro. As S. pyogenes lacks the oxidative part of the pentose phosphate pathway, GapN appears to be the major NADPH source for the bacterium. Accordingly, other streptococci that carry a complete pentose phosphate pathway are not prone to asPNA-based gapN knock-down. Determination of the crystal structure of the S. pyogenes GapN apo-enzyme revealed an unusual cis-peptide in proximity to the catalytic binding site. Furthermore, using a structural modeling approach, we correctly predicted competitive inhibition of S. pyogenes GapN by erythrose 4-phosphate, indicating that our structural model can be used for in silico screening of specific GapN inhibitors. In conclusion, the data provided here reveal that GapN is a potential target for antimicrobial substances that selectively kill S. pyogenes and other streptococci that lack the oxidative part of the pentose phosphate pathway. | ||
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| + | The Non-phosphorylating Glyceraldehyde-3-Phosphate Dehydrogenase GapN Is a Potential New Drug Target in Streptococcus pyogenes.,Eisenberg P, Albert L, Teuffel J, Zitzow E, Michaelis C, Jarick J, Sehlke C, Grosse L, Bader N, Nunes-Alves A, Kreikemeyer B, Schindelin H, Wade RC, Fiedler T Front Microbiol. 2022 Feb 15;13:802427. doi: 10.3389/fmicb.2022.802427., eCollection 2022. PMID:35242116<ref>PMID:35242116</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7pkj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus pyogenes M49 591]] | ||
[[Category: Albert L]] | [[Category: Albert L]] | ||
[[Category: Schindelin H]] | [[Category: Schindelin H]] | ||
Revision as of 13:06, 1 February 2024
Streptococcus pyogenes apo GapN
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