7e6h: Difference between revisions
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==glucose-6-phosphate dehydrogenase from Kluyveromyces lactis== | ==glucose-6-phosphate dehydrogenase from Kluyveromyces lactis== | ||
<StructureSection load='7e6h' size='340' side='right'caption='[[7e6h]]' scene=''> | <StructureSection load='7e6h' size='340' side='right'caption='[[7e6h]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E6H FirstGlance]. <br> | <table><tr><td colspan='2'>[[7e6h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E6H FirstGlance]. <br> | ||
</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=7e6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e6h OCA], [https://pdbe.org/7e6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e6h RCSB], [https://www.ebi.ac.uk/pdbsum/7e6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e6h ProSAT]</span></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]] 2.7Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7PE:2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHANOL'>7PE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=7e6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e6h OCA], [https://pdbe.org/7e6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e6h RCSB], [https://www.ebi.ac.uk/pdbsum/7e6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e6h ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/G6PD_KLULA G6PD_KLULA] Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).[UniProtKB:P11413] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glucose-6-phosphate dehydrogenase is the first enzyme in the pentose phosphate pathway. The reaction catalyzed by the enzyme is considered to be the main source of reducing power for nicotinamide adenine dinucleotide phosphate (NADPH) and is a precursor of 5-carbon sugar used by cells. To uncover the structural features of the enzyme, we determined the crystal structures of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis (KlG6PD) in both the apo form and a binary complex with its substrate glucose-6-phosphate. KlG6PD contains a Rossman-like domain for cofactor NADPH binding; it also presents a typical antiparallel beta sheet at the C-terminal domain with relatively the same pattern as those of other homologous structures. Moreover, our structural and biochemical analyses revealed that Lys153 contributes significantly to substrate G6P recognition. This study may provide insights into the structural variation and catalytic features of the G6PD enzyme. | |||
Structural basis for substrate recognition of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis.,Vu HH, Jin C, Chang JH Biochem Biophys Res Commun. 2021 Mar 22;553:85-91. doi:, 10.1016/j.bbrc.2021.02.088. PMID:33765558<ref>PMID:33765558</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7e6h" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Kluyveromyces lactis NRRL Y-1140]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chang JH]] | [[Category: Chang JH]] | ||
[[Category: Ha VH]] | [[Category: Ha VH]] | ||
Latest revision as of 19:47, 29 November 2023
glucose-6-phosphate dehydrogenase from Kluyveromyces lactisglucose-6-phosphate dehydrogenase from Kluyveromyces lactis
Structural highlights
FunctionG6PD_KLULA Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).[UniProtKB:P11413] Publication Abstract from PubMedGlucose-6-phosphate dehydrogenase is the first enzyme in the pentose phosphate pathway. The reaction catalyzed by the enzyme is considered to be the main source of reducing power for nicotinamide adenine dinucleotide phosphate (NADPH) and is a precursor of 5-carbon sugar used by cells. To uncover the structural features of the enzyme, we determined the crystal structures of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis (KlG6PD) in both the apo form and a binary complex with its substrate glucose-6-phosphate. KlG6PD contains a Rossman-like domain for cofactor NADPH binding; it also presents a typical antiparallel beta sheet at the C-terminal domain with relatively the same pattern as those of other homologous structures. Moreover, our structural and biochemical analyses revealed that Lys153 contributes significantly to substrate G6P recognition. This study may provide insights into the structural variation and catalytic features of the G6PD enzyme. Structural basis for substrate recognition of glucose-6-phosphate dehydrogenase from Kluyveromyces lactis.,Vu HH, Jin C, Chang JH Biochem Biophys Res Commun. 2021 Mar 22;553:85-91. doi:, 10.1016/j.bbrc.2021.02.088. PMID:33765558[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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