4fh1
From Proteopedia
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| - | + | ==S. cerevisiae Ubc13-N79A== | |
| - | === | + | <StructureSection load='4fh1' size='340' side='right' caption='[[4fh1]], [[Resolution|resolution]] 2.61Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4fh1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FH1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBC13, YDR092W, YD6652.04 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=4fh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fh1 RCSB], [http://www.ebi.ac.uk/pdbsum/4fh1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | It is widely accepted that ubiquitin-conjugating enzymes contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of the conserved asparagine to ubiquitin conjugation by Ubc13-Mms2, we conclude that the importance of this residue stems primarily from its structural role in stabilizing an active site loop. | ||
| - | + | A conserved asparagine has a structural role in ubiquitin-conjugating enzymes.,Berndsen CE, Wiener R, Yu IW, Ringel AE, Wolberger C Nat Chem Biol. 2013 Mar;9(3):154-6. doi: 10.1038/nchembio.1159. Epub 2013 Jan 6. PMID:23292652<ref>PMID:23292652</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Ubiquitin conjugating enzyme|Ubiquitin conjugating enzyme]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae s288c]] | [[Category: Saccharomyces cerevisiae s288c]] | ||
[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
| - | [[Category: Berndsen, C E | + | [[Category: Berndsen, C E]] |
| - | [[Category: Wiener, R | + | [[Category: Wiener, R]] |
| - | [[Category: Wolberger, C | + | [[Category: Wolberger, C]] |
[[Category: Ligase]] | [[Category: Ligase]] | ||
[[Category: Ubiquitin conjugating enzyme]] | [[Category: Ubiquitin conjugating enzyme]] | ||
Revision as of 11:19, 21 December 2014
S. cerevisiae Ubc13-N79A
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