3fxe
From Proteopedia
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| - | [[ | + | ==Crystal structure of interacting domains of IcmR and IcmQ (seleno-derivative)== |
| + | <StructureSection load='3fxe' size='340' side='right' caption='[[3fxe]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3fxe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila] and [http://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._philadelphia_1 Legionella pneumophila subsp. pneumophila str. philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FXE FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">icmQ, LPC_2899 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 Legionella pneumophila]), icmR, lpg0443 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 Legionella pneumophila subsp. pneumophila str. Philadelphia 1])</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=3fxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fxe RCSB], [http://www.ebi.ac.uk/pdbsum/3fxe 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/fx/3fxe_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 == | ||
| + | During infection, Legionella pneumophila creates a replication vacuole within eukaryotic cells and this requires a Type IVb secretion system (T4bSS). IcmQ plays a critical role in the translocase and associates with IcmR. In this paper, we show that the N-terminal domain of IcmQ (Qn) mediates self-dimerization, whereas the C-terminal domain with a basic linker promotes membrane association. In addition, the binding of IcmR to IcmQ prevents self-dimerization and also blocks membrane permeabilization. However, IcmR does not completely block membrane binding by IcmQ. We then determined crystal structures of Qn with the interacting region of IcmR. In this complex, each protein forms an alpha-helical hairpin within a parallel four-helix bundle. The amphipathic nature of helices in Qn suggests two possible models for membrane permeabilization by IcmQ. The Rm-Qn structure also suggests how IcmR-like proteins in other L. pneumophila species may interact with their IcmQ partners. | ||
| - | + | Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila.,Raychaudhury S, Farelli JD, Montminy TP, Matthews M, Menetret JF, Dumenil G, Roy CR, Head JF, Isberg RR, Akey CW Structure. 2009 Apr 15;17(4):590-601. PMID:19368892<ref>PMID:19368892</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Legionella pneumophila]] | [[Category: Legionella pneumophila]] | ||
[[Category: Legionella pneumophila subsp. pneumophila str. philadelphia 1]] | [[Category: Legionella pneumophila subsp. pneumophila str. philadelphia 1]] | ||
| - | [[Category: Akey, C W | + | [[Category: Akey, C W]] |
| - | [[Category: Head, J F | + | [[Category: Head, J F]] |
| - | [[Category: Raychaudhury, S | + | [[Category: Raychaudhury, S]] |
| - | [[Category: | + | [[Category: Helix bundle]] |
[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
[[Category: Se-met]] | [[Category: Se-met]] | ||
[[Category: Unknown function]] | [[Category: Unknown function]] | ||
Revision as of 10:19, 3 December 2014
Crystal structure of interacting domains of IcmR and IcmQ (seleno-derivative)
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