5za0: Difference between revisions
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The | ==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 [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='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='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'>[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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G3P1_ECOLI G3P1_ECOLI] | |||
<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> | |||
==See Also== | |||
*[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Kim YJ]] | |||