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| | <StructureSection load='5za0' size='340' side='right'caption='[[5za0]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5za0' size='340' side='right'caption='[[5za0]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5za0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZA0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZA0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5za0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZA0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <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]] 2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</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'>[http://proteopedia.org/fgij/fg.htm?mol=5za0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5za0 OCA], [http://pdbe.org/5za0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5za0 RCSB], [http://www.ebi.ac.uk/pdbsum/5za0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5za0 ProSAT]</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=5za0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5za0 OCA], [https://pdbe.org/5za0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5za0 RCSB], [https://www.ebi.ac.uk/pdbsum/5za0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5za0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G3P1_ECOLI G3P1_ECOLI] |
| | <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: Escherichia coli k-12]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kim, Y J]] | + | [[Category: Kim YJ]] |
| - | [[Category: Cryo-protectant]]
| + | |
| - | [[Category: Glycolysis]]
| + | |
| - | [[Category: Hypothetical]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
G3P1_ECOLI
Publication Abstract from PubMed
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, catalyses the conversion of D-glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. While mammalian and yeast GAPDHs are multifunctional proteins that have additional functions beyond those involved in glycolysis, including reactions related to nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis, Escherichia coli GAPDH (ecGAPDH) has only been reported to function in glycolysis. The S-loop of GAPDH is required for interaction with its cofactor and with other proteins. In this study, the three-dimensional crystal structure of GAPDH treated with trehalose is reported at 2.0 A resolution. Trehalose was used as a cryoprotectant for the GAPDH crystals. The structure of trehalose-bound ecGAPDH was compared with the structures of both NAD(+)-free and NAD(+)-bound ecGAPDH. At the S-loop, the bound trehalose in the GAPDH structure induces a 2.4 degrees rotation compared with the NAD(+)-free ecGAPDH structure and a 3.1 degrees rotation compared with the NAD(+)-bound ecGAPDH structure.
A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.,Kim YJ Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):277-282. doi:, 10.1107/S2053230X18004557. Epub 2018 Apr 16. PMID:29717994[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim YJ. A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase. Acta Crystallogr F Struct Biol Commun. 2018 May 1;74(Pt 5):277-282. doi:, 10.1107/S2053230X18004557. Epub 2018 Apr 16. PMID:29717994 doi:http://dx.doi.org/10.1107/S2053230X18004557
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