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2px9
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="2px9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2px9" /> '''The intrinsic affinity between E2 and the C...) |
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| - | [[Image:2px9.gif|left|200px]]<br /> | ||
| - | <applet load="2px9" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2px9" /> | ||
| - | '''The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications'''<br /> | ||
| - | == | + | ==The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications== |
| - | Ubiquitin-like modifications, which are carried out by similar biochemical | + | <StructureSection load='2px9' size='340' side='right'caption='[[2px9]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2px9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PX9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2px9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2px9 OCA], [https://pdbe.org/2px9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2px9 RCSB], [https://www.ebi.ac.uk/pdbsum/2px9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2px9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SAE2_HUMAN SAE2_HUMAN] The heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.<ref>PMID:11481243</ref> <ref>PMID:11451954</ref> <ref>PMID:19443651</ref> <ref>PMID:15660128</ref> <ref>PMID:17643372</ref> <ref>PMID:20164921</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/px/2px9_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=2px9 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ubiquitin-like modifications, which are carried out by similar biochemical mechanisms, regulate nearly every aspect of cellular function. Despite the recent advancements in characterizing their enzymology, our knowledge about the dynamic processes of these modifications is still fragmentary. In this study, we have uncovered an intrinsic affinity between the SUMO E2 and the Cys domain of SUMO E1. NMR studies in combination with paramagnetic spin labeling demonstrate that this interaction is mediated by previously unknown interfaces on both E1 and E2 and places the two catalytic Cys residues of the two enzymes in close proximity. Site-directed mutagenesis and enzymatic assays indicate that the interaction is fundamentally important for the transfer of SUMO from E1 to E2. Results from this study suggest that the interaction between E2 and the Cys domain of E1 participates in guiding the E2's translocation to E1's enzymatic active site in ubiquitin-like modifications. | ||
| - | + | The intrinsic affinity between E2 and the Cys domain of E1 in ubiquitin-like modifications.,Wang J, Hu W, Cai S, Lee B, Song J, Chen Y Mol Cell. 2007 Jul 20;27(2):228-37. PMID:17643372<ref>PMID:17643372</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2px9" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cai S]] | ||
| + | [[Category: Chen Y]] | ||
| + | [[Category: Hu WD]] | ||
| + | [[Category: Lee B]] | ||
| + | [[Category: Song J]] | ||
| + | [[Category: Wang JH]] | ||
Current revision
The intrinsic affinity between E2 and the Cys domain of E1 in Ubiquitin-like modifications
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Categories: Homo sapiens | Large Structures | Cai S | Chen Y | Hu WD | Lee B | Song J | Wang JH
