3l3p
From Proteopedia
(Difference between revisions)
m (Protected "3l3p" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap== | |
| - | + | <StructureSection load='3l3p' size='340' side='right' caption='[[3l3p]], [[Resolution|resolution]] 3.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3l3p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L3P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L3P FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ckd|3ckd]], [[3cvr|3cvr]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ipaH9.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 Shigella flexneri])</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=3l3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l3p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l3p RCSB], [http://www.ebi.ac.uk/pdbsum/3l3p PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/l3/3l3p_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We show that the monomeric form of Shigella IpaH9.8 E3 ligase catalyses the ubiquitination of human U2AF35 in vitro, providing a molecular mechanism for the observed in vivo effect. We further discover that under non-reducing conditions IpaH9.8 undergoes a domain swap driven by the formation of a disulfide bridge involving the catalytic cysteine and that this dimer is unable to catalyse the ubiquitination of U2AF35. The crystal structure of the domain-swapped dimer is presented. The redox inactivation of IpaH9.8 could be a mechanism of regulating the activity of the IpaH9.8 E3 ligase in response to cell damage so that the host cell in which the bacteria resides is maintained in a benign state suitable for bacterial survival. | ||
| - | + | A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase.,Seyedarabi A, Sullivan JA, Sasakawa C, Pickersgill RW FEBS Lett. 2010 Oct 8;584(19):4163-8. Epub 2010 Sep 8. PMID:20831869<ref>PMID:20831869</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Shigella flexneri]] | [[Category: Shigella flexneri]] | ||
[[Category: Ubiquitin--protein ligase]] | [[Category: Ubiquitin--protein ligase]] | ||
| - | [[Category: Pickersgill, R W | + | [[Category: Pickersgill, R W]] |
| - | [[Category: Sasakawa, C | + | [[Category: Sasakawa, C]] |
| - | [[Category: Seyedarabi, A | + | [[Category: Seyedarabi, A]] |
| - | [[Category: Sullivan, J A | + | [[Category: Sullivan, J A]] |
[[Category: Cxd motif]] | [[Category: Cxd motif]] | ||
[[Category: Domain swap]] | [[Category: Domain swap]] | ||
[[Category: E3 ligase]] | [[Category: E3 ligase]] | ||
[[Category: Ligase]] | [[Category: Ligase]] | ||
Revision as of 16:07, 18 December 2014
Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap
| |||||||||||
