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| <StructureSection load='4qx6' size='340' side='right'caption='[[4qx6]], [[Resolution|resolution]] 2.46Å' scene=''> | | <StructureSection load='4qx6' size='340' side='right'caption='[[4qx6]], [[Resolution|resolution]] 2.46Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4qx6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Stra3 Stra3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QX6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qx6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_NEM316 Streptococcus agalactiae NEM316]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QX6 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k73|3k73]]</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=4qx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qx6 OCA], [https://pdbe.org/4qx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qx6 RCSB], [https://www.ebi.ac.uk/pdbsum/4qx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qx6 ProSAT]</span></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gapC; GBS 1811, gbs1811 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211110 STRA3])</td></tr>
| + | |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </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=4qx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qx6 OCA], [http://pdbe.org/4qx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qx6 RCSB], [http://www.ebi.ac.uk/pdbsum/4qx6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qx6 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q8E3E8_STRA3 Q8E3E8_STRA3] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | |
| ==See Also== | | ==See Also== |
- | *[[Glyceraldehyde-3-Phosphate Dehydrogenase|Glyceraldehyde-3-Phosphate Dehydrogenase]] | + | *[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Stra3]] | + | [[Category: Streptococcus agalactiae NEM316]] |
- | [[Category: Ayres, C A]] | + | [[Category: Ayres CA]] |
- | [[Category: Banerjee, S]] | + | [[Category: Banerjee S]] |
- | [[Category: Chattopadhyay, D]] | + | [[Category: Chattopadhyay D]] |
- | [[Category: Schormann, N]] | + | [[Category: Schormann N]] |
- | [[Category: Gapdh]]
| + | |
- | [[Category: Glycolysis]]
| + | |
- | [[Category: Nad]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q8E3E8_STRA3
Publication Abstract from PubMed
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a conserved cytosolic enzyme, which plays a key role in glycolysis. GAPDH catalyzes the oxidative phosphorylation of D-glyceraldehyde 3-phosphate using NAD or NADP as a cofactor. In addition, GAPDH localized on the surface of some bacteria is thought to be involved in macromolecular interactions and bacterial pathogenesis. GAPDH on the surface of group B streptococcus (GBS) enhances bacterial virulence and is a potential vaccine candidate. Here, the crystal structure of GBS GAPDH from Streptococcus agalactiae in complex with NAD is reported at 2.46 A resolution. Although the overall structure of GBS GAPDH is very similar to those of other GAPDHs, the crystal structure reveals a significant difference in the area spanning residues 294-307, which appears to be more acidic. The amino-acid sequence of this region of GBS GAPDH is also distinct compared with other GAPDHs. This region therefore may be of interest as an immunogen for vaccine development.
Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface.,Ayres CA, Schormann N, Senkovich O, Fry A, Banerjee S, Ulett GC, Chattopadhyay D Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1333-9. doi:, 10.1107/S2053230X14019517. Epub 2014 Sep 25. PMID:25286935[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ayres CA, Schormann N, Senkovich O, Fry A, Banerjee S, Ulett GC, Chattopadhyay D. Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1333-9. doi:, 10.1107/S2053230X14019517. Epub 2014 Sep 25. PMID:25286935 doi:http://dx.doi.org/10.1107/S2053230X14019517
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