2r45

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[[Image:2r45.jpg|left|200px]]
 
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==Crystal structure of Escherichia coli Glycerol-3-phosphate Dehydrogenase in complex with 2-phospho-d-glyceric acid==
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The line below this paragraph, containing "STRUCTURE_2r45", creates the "Structure Box" on the page.
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<StructureSection load='2r45' size='340' side='right'caption='[[2r45]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2r45]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R45 FirstGlance]. <br>
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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]] 2.3&#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=2PG:2-PHOSPHOGLYCERIC+ACID'>2PG</scene>, <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=T3A:N-(TRIS(HYDROXYMETHYL)METHYL)-3-AMINOPROPANESULFONIC+ACID'>T3A</scene></td></tr>
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{{STRUCTURE_2r45| PDB=2r45 | SCENE= }}
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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=2r45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r45 OCA], [https://pdbe.org/2r45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r45 RCSB], [https://www.ebi.ac.uk/pdbsum/2r45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r45 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLPD_ECOLI GLPD_ECOLI] Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/2r45_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r45 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of Escherichia coli Glycerol-3-phosphate Dehydrogenase in complex with 2-phospho-d-glyceric acid'''
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==See Also==
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*[[Glycerol-3-phosphate dehydrogenase 3D structures|Glycerol-3-phosphate dehydrogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Sn-glycerol-3-phosphate dehydrogenase (GlpD) is an essential membrane enzyme, functioning at the central junction of respiration, glycolysis, and phospholipid biosynthesis. Its critical role is indicated by the multitiered regulatory mechanisms that stringently controls its expression and function. Once expressed, GlpD activity is regulated through lipid-enzyme interactions in Escherichia coli. Here, we report seven previously undescribed structures of the fully active E. coli GlpD, up to 1.75 A resolution. In addition to elucidating the structure of the native enzyme, we have determined the structures of GlpD complexed with substrate analogues phosphoenolpyruvate, glyceric acid 2-phosphate, glyceraldehyde-3-phosphate, and product, dihydroxyacetone phosphate. These structural results reveal conformational states of the enzyme, delineating the residues involved in substrate binding and catalysis at the glycerol-3-phosphate site. Two probable mechanisms for catalyzing the dehydrogenation of glycerol-3-phosphate are envisioned, based on the conformational states of the complexes. To further correlate catalytic dehydrogenation to respiration, we have additionally determined the structures of GlpD bound with ubiquinone analogues menadione and 2-n-heptyl-4-hydroxyquinoline N-oxide, identifying a hydrophobic plateau that is likely the ubiquinone-binding site. These structures illuminate probable mechanisms of catalysis and suggest how GlpD shuttles electrons into the respiratory pathway. Glycerol metabolism has been implicated in insulin signaling and perturbations in glycerol uptake and catabolism are linked to obesity in humans. Homologs of GlpD are found in practically all organisms, from prokaryotes to humans, with &gt;45% consensus protein sequences, signifying that these structural results on the prokaryotic enzyme may be readily applied to the eukaryotic GlpD enzymes.
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==About this Structure==
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2R45 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R45 OCA].
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==Reference==
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Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism., Yeh JI, Chinte U, Du S, Proc Natl Acad Sci U S A. 2008 Mar 4;105(9):3280-5. Epub 2008 Feb 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18296637 18296637]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Glycerol-3-phosphate dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chinte U]]
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[[Category: Chinte, U.]]
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[[Category: Du S]]
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[[Category: Du, S.]]
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[[Category: Yeh JI]]
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[[Category: Yeh, J I.]]
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[[Category: Glpd]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:05:46 2008''
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Current revision

Crystal structure of Escherichia coli Glycerol-3-phosphate Dehydrogenase in complex with 2-phospho-d-glyceric acid

PDB ID 2r45

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