2pfg
From Proteopedia
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(New page: 200px<br /> <applet load="2pfg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pfg, resolution 1.54Å" /> '''Crystal structure o...) |
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| - | [[Image:2pfg.gif|left|200px]]<br /> | ||
| - | <applet load="2pfg" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2pfg, resolution 1.54Å" /> | ||
| - | '''Crystal structure of human CBR1 in complex with BiGF2.'''<br /> | ||
| - | == | + | ==Crystal structure of human CBR1 in complex with BiGF2.== |
| - | Glutathione forms complex reaction products with formaldehyde, which can | + | <StructureSection load='2pfg' size='340' side='right'caption='[[2pfg]], [[Resolution|resolution]] 1.54Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2pfg]] is a 1 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=2PFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PFG 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]] 1.54Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DDD:(5R,10S)-5-{[(CARBOXYMETHYL)AMINO]CARBONYL}-7-OXO-3-THIA-1,6-DIAZABICYCLO[4.4.1]UNDECANE-10-CARBOXYLIC+ACID'>DDD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M0H:S-(HYDROXYMETHYL)-L-CYSTEINE'>M0H</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=2pfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pfg OCA], [https://pdbe.org/2pfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pfg RCSB], [https://www.ebi.ac.uk/pdbsum/2pfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pfg ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CBR1_HUMAN CBR1_HUMAN] NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds doxorubicinol and daunorubicinol. Can convert prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione, which explains its higher affinity for glutathione-conjugated substrates. Catalyzes the reduction of S-nitrosoglutathione.<ref>PMID:18449627</ref> <ref>PMID:15799708</ref> <ref>PMID:17912391</ref> <ref>PMID:18826943</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/2pfg_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2pfg ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glutathione forms complex reaction products with formaldehyde, which can be further modified through enzymatic modification. We studied the non-enzymatic reaction between glutathione and formaldehyde and identified a bicyclic complex containing two equivalents of formaldehyde and one glutathione molecule by protein X-ray crystallography (PDB accession number 2PFG). We have also used (1)H, (13)C and 2D NMR spectroscopy to confirm the structure of this unusual adduct. The key feature of this adduct is the involvement of the gamma-glutamyl alpha-amine and the Cys thiol in the formation of the bicyclic ring structure. These findings suggest that the structure of GSH allows for bi-dentate masking of the reactivity of formaldehyde. As this species predominates at near physiological pH values, we suggest this adduct may have biological significance. | ||
| - | + | Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct.,Bateman R, Rauh D, Shokat KM Org Biomol Chem. 2007 Oct 21;5(20):3363-7. Epub 2007 Aug 29. PMID:17912391<ref>PMID:17912391</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2pfg" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bateman RL]] | ||
| + | [[Category: Rauh D]] | ||
| + | [[Category: Shokat KM]] | ||
Current revision
Crystal structure of human CBR1 in complex with BiGF2.
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