7c5f

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==Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 1.88 Angstrom resolution==
==Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 1.88 Angstrom resolution==
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<StructureSection load='7c5f' size='340' side='right'caption='[[7c5f]]' scene=''>
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<StructureSection load='7c5f' size='340' side='right'caption='[[7c5f]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C5F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7C5F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7c5f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C5F FirstGlance]. <br>
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</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=7c5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c5f OCA], [http://pdbe.org/7c5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7c5f RCSB], [http://www.ebi.ac.uk/pdbsum/7c5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7c5f ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7c5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c5f OCA], [https://pdbe.org/7c5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c5f RCSB], [https://www.ebi.ac.uk/pdbsum/7c5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c5f ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A140NCK4_ECOBD A0A140NCK4_ECOBD] Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.[ARBA:ARBA00003501]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme in the glycolytic pathway that catalyzes the conversion of D-glyceraldehyde 3-phosphate to 1,3-diphosphoglycerate. Here, the full-length GAPDH type 1 from Escherichia coli (EcGAPDH1) was cloned and overexpressed, and the protein was purified. Biochemical analyses found that the optimum reaction temperature and pH of EcGAPDH1 were 55 degrees C and 10.0, respectively. The protein has a certain amount of thermostability. Crystals of EcGAPDH1 were obtained using the sitting-drop vapor-diffusion technique and X-ray diffraction data were collected to 1.88 A resolution. Characterization of the crystals showed that they belonged to space group P41212, with unit-cell parameters a = b = 89.651, c = 341.007 A, alpha = beta = gamma = 90 degrees . The structure of EcGAPDH1 contains four subunits, each of which includes an N-terminal NAD(+)-binding domain and a C-terminal catalytic domain. Analysis of the NAD(+)-bound form showed some differences between the structures of EcGAPDH1 and human GAPDH. As EcGAPDH1 shares 100% identity with GAPDH from Shigella sonnei, its structure may help in finding a drug for the treatment of shigellosis.
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Characterization and structure of glyceraldehyde-3-phosphate dehydrogenase type 1 from Escherichia coli.,Zhang L, Liu MR, Yao YC, Bostrom IK, Wang YD, Chen AQ, Li JX, Gu SH, Ji CN Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):406-413. doi:, 10.1107/S2053230X20010067. Epub 2020 Aug 19. PMID:32880588<ref>PMID:32880588</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7c5f" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal Structure of Glyceraldehyde-3-phosphate dehydrogenase1 from Escherichia coli at 1.88 Angstrom resolution

PDB ID 7c5f

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