5za0
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==A cryo-protectant induces the conformational change of glyceraldehyde-3-phosphate dehydrogenase== | |
| + | <StructureSection load='5za0' size='340' side='right' caption='[[5za0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZA0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRE:TREHALOSE'>TRE</scene></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=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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:29717994</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5za0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli k-12]] | ||
| + | [[Category: Kim, Y J]] | ||
| + | [[Category: Cryo-protectant]] | ||
| + | [[Category: Glycolysis]] | ||
| + | [[Category: Hypothetical]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 05:30, 30 May 2018
A cryo-protectant induces the conformational change of glyceraldehyde-3-phosphate dehydrogenase
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