This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4gr1
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="4gr1" size="450" color="white" frame="true" align="right" spinBox="true" caption="4gr1, resolution 2.4Å" /> '''THE BINDING OF THE R...) |
|||
| (12 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:4gr1.gif|left|200px]]<br /> | ||
| - | <applet load="4gr1" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="4gr1, resolution 2.4Å" /> | ||
| - | '''THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE'''<br /> | ||
| - | == | + | ==THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE== |
| - | The retro-analogue of glutathione disulfide was bound to the GSSG binding | + | <StructureSection load='4gr1' size='340' side='right'caption='[[4gr1]], [[Resolution|resolution]] 2.40Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4gr1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GR1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RGS:4N-MALONYL-CYSTEINYL-2,4-DIAMINOBUTYRATE+DISULFIDE'>RGS</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione-disulfide_reductase Glutathione-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.7 1.8.1.7] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gr1 OCA], [http://pdbe.org/4gr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4gr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gr1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GSHR_HUMAN GSHR_HUMAN]] Maintains high levels of reduced glutathione in the cytosol. | ||
| + | == 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/gr/4gr1_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=4gr1 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained. | ||
| - | + | The binding of the retro-analogue of glutathione disulfide to glutathione reductase.,Janes W, Schulz GE J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009<ref>PMID:2355009</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 4gr1" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Glutathione Reductase|Glutathione Reductase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Glutathione-disulfide reductase]] | [[Category: Glutathione-disulfide reductase]] | ||
| - | [[Category: | + | [[Category: Human]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Janes, W | + | [[Category: Janes, W]] |
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE
| |||||||||||
