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| | ==Crystal structure of interacting domains of IcmR and IcmQ== | | ==Crystal structure of interacting domains of IcmR and IcmQ== |
| - | <StructureSection load='3fxd' size='340' side='right' caption='[[3fxd]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3fxd' size='340' side='right'caption='[[3fxd]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fxd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Legpc Legpc] and [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FXD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fxd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_str._Corby Legionella pneumophila str. Corby] and [https://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=3FXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FXD FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fxe|3fxe]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=400673 LEGPC]), icmR, lpg0443 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</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=3fxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxd OCA], [https://pdbe.org/3fxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fxd RCSB], [https://www.ebi.ac.uk/pdbsum/3fxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxd ProSAT]</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=3fxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fxd OCA], [http://pdbe.org/3fxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fxd RCSB], [http://www.ebi.ac.uk/pdbsum/3fxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3fxd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5ZYC9_LEGPH Q5ZYC9_LEGPH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Legpc]] | + | [[Category: Large Structures]] |
| - | [[Category: Legph]] | + | [[Category: Legionella pneumophila str. Corby]] |
| - | [[Category: Akey, C W]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| - | [[Category: Head, J F]] | + | [[Category: Akey CW]] |
| - | [[Category: Raychaudhury, S]] | + | [[Category: Head JF]] |
| - | [[Category: Helix bundle]] | + | [[Category: Raychaudhury S]] |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Q5ZYC9_LEGPH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Raychaudhury S, Farelli JD, Montminy TP, Matthews M, Menetret JF, Dumenil G, Roy CR, Head JF, Isberg RR, Akey CW. Structure and function of interacting IcmR-IcmQ domains from a type IVb secretion system in Legionella pneumophila. Structure. 2009 Apr 15;17(4):590-601. PMID:19368892 doi:10.1016/j.str.2009.02.011
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