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| | <StructureSection load='3ovp' size='340' side='right'caption='[[3ovp]], [[Resolution|resolution]] 1.69Å' scene=''> | | <StructureSection load='3ovp' size='340' side='right'caption='[[3ovp]], [[Resolution|resolution]] 1.69Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ovp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OVP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ovp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OVP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=XPE:3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL'>XPE</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]] 1.695Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ovq|3ovq]], [[3ovr|3ovr]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=XPE:3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL'>XPE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPE, HUSSY-17 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribulose-phosphate_3-epimerase Ribulose-phosphate 3-epimerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.3.1 5.1.3.1] </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=3ovp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ovp OCA], [https://pdbe.org/3ovp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ovp RCSB], [https://www.ebi.ac.uk/pdbsum/3ovp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ovp 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=3ovp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ovp OCA], [https://pdbe.org/3ovp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ovp RCSB], [https://www.ebi.ac.uk/pdbsum/3ovp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ovp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/RPE_HUMAN RPE_HUMAN]] Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.<ref>PMID:20923965</ref>
| + | [https://www.uniprot.org/uniprot/RPE_HUMAN RPE_HUMAN] Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.<ref>PMID:20923965</ref> |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ribulose-phosphate 3-epimerase]]
| + | [[Category: Joachimiak A]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Liang WG]] |
| - | [[Category: Liang, W G]] | + | [[Category: Liu ZJ]] |
| - | [[Category: Liu, Z J]] | + | [[Category: Ouyang SY]] |
| - | [[Category: Ouyang, S Y]] | + | [[Category: Shaw N]] |
| - | [[Category: Shaw, N]] | + | [[Category: Zhang RG]] |
| - | [[Category: Zhang, R G]] | + | |
| - | [[Category: Iron binding]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
RPE_HUMAN Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.[1]
Publication Abstract from PubMed
The pentose phosphate pathway (PPP) confers protection against oxidative stress by supplying NADPH necessary for the regeneration of glutathione, which detoxifies H(2)O(2) into H(2)O and O(2). RPE functions in the PPP, catalyzing the reversible conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate and is an important enzyme for cellular response against oxidative stress. Here, using structural, biochemical, and functional studies, we show that human D-ribulose 5-phosphate 3-epimerase (hRPE) uses Fe(2+) for catalysis. Structures of the binary complexes of hRPE with D-ribulose 5-phosphate and D-xylulose 5-phosphate provide the first detailed molecular insights into the binding mode of physiological ligands and reveal an octahedrally coordinated Fe(2+) ion buried deep inside the active site. Human RPE folds into a typical (beta/alpha)(8) triosephosphate isomerase (TIM) barrel with a loop regulating access to the active site. Two aspartic acids are well positioned to carry out the proton transfers in an acid-base type of reaction mechanism. Interestingly, mutating Ser-10 to alanine almost abolished the enzymatic activity, while L12A and M72A mutations resulted in an almost 50% decrease in the activity. The binary complexes of hRPE reported here will aid in the design of small molecules for modulating the activity of the enzyme and altering flux through the PPP.
Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE.,Liang W, Ouyang S, Shaw N, Joachimiak A, Zhang R, Liu ZJ FASEB J. 2011 Feb;25(2):497-504. Epub 2010 Oct 5. PMID:20923965[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liang W, Ouyang S, Shaw N, Joachimiak A, Zhang R, Liu ZJ. Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE. FASEB J. 2011 Feb;25(2):497-504. Epub 2010 Oct 5. PMID:20923965 doi:10.1096/fj.10-171207
- ↑ Liang W, Ouyang S, Shaw N, Joachimiak A, Zhang R, Liu ZJ. Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE. FASEB J. 2011 Feb;25(2):497-504. Epub 2010 Oct 5. PMID:20923965 doi:10.1096/fj.10-171207
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