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| | <StructureSection load='5jy6' size='340' side='right'caption='[[5jy6]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5jy6' size='340' side='right'caption='[[5jy6]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jy6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptoccocus_de_la_mammite"_nocard_and_mollereau_1887 "streptoccocus de la mammite" nocard and mollereau 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JY6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JY6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jy6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JY6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jyf|5jyf]], [[5jye|5jye]], [[5jya|5jya]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gap, gapA, EN72_09590, ERS039640_00200, ERS046921_00390, RDF_1710 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1311 "Streptoccocus de la mammite" Nocard and Mollereau 1887])</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=5jy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jy6 OCA], [https://pdbe.org/5jy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jy6 RCSB], [https://www.ebi.ac.uk/pdbsum/5jy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jy6 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=5jy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jy6 OCA], [http://pdbe.org/5jy6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jy6 RCSB], [http://www.ebi.ac.uk/pdbsum/5jy6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jy6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9ALW2_STRAG Q9ALW2_STRAG] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptoccocus de la mammite nocard and mollereau 1887]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chattopadhyay, D]] | + | [[Category: Streptococcus agalactiae]] |
| - | [[Category: Schormann, N]] | + | [[Category: Chattopadhyay D]] |
| - | [[Category: Gapdh]] | + | [[Category: Schormann N]] |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
Q9ALW2_STRAG
Publication Abstract from PubMed
Glyceraldehyde 3-phosphate dehydrogenase or GAPDH is an evolutionarily conserved glycolytic enzyme. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and NAD+ as cofactor. GAPDH of Group B Streptococcus is a major virulence factor and a potential vaccine candidate. Moreover, since GAPDH activity is essential for bacterial growth it may serve as a possible drug target. Crystal structures of Group B Streptococcus GAPDH in the apo-form, two different binary complexes and the ternary complex are described here. The two binary complexes contained NAD+ bound to 2 (mixed-holo) or 4 (holo) subunits of the tetrameric protein. The structure of the mixed-holo complex reveals the effects of NAD+ binding on the conformation of the protein. In the ternary complex, the phosphate group of the substrate was bound to the new Pi site in all four subunits. Comparison with the structure of human GAPDH showed several differences near the adenosyl binding pocket in Group B Streptococcus GAPDH. The structures also reveal at least three surface-exposed areas that differ in amino acid sequence compared to the corresponding areas of human GAPDH.
Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes.,Schormann N, Ayres CA, Fry A, Green TJ, Banerjee S, Ulett GC, Chattopadhyay D PLoS One. 2016 Nov 22;11(11):e0165917. doi: 10.1371/journal.pone.0165917., eCollection 2016. PMID:27875551[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schormann N, Ayres CA, Fry A, Green TJ, Banerjee S, Ulett GC, Chattopadhyay D. Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes. PLoS One. 2016 Nov 22;11(11):e0165917. doi: 10.1371/journal.pone.0165917., eCollection 2016. PMID:27875551 doi:http://dx.doi.org/10.1371/journal.pone.0165917
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