4mu6
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of the N-terminal domain of Effector Protein LegC3 from Legionella pneumophila== | |
| + | <StructureSection load='4mu6' size='340' side='right'caption='[[4mu6]], [[Resolution|resolution]] 2.08Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mu6]] is a 1 chain structure with sequence from [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=4MU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MU6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.082Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4mu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mu6 OCA], [https://pdbe.org/4mu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mu6 RCSB], [https://www.ebi.ac.uk/pdbsum/4mu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mu6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q5ZUU1_LEGPH Q5ZUU1_LEGPH] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Legionella pneumophila secretes over 300 effectors during the invasion of human cells. The functions of only a small number of them have been identified. LegC3 is one of the identified effectors, which is believed to act by inhibiting vacuolar fusion. It contains two predicted transmembrane helices that divide the protein into a larger N-terminal domain and a smaller C-terminal domain. The function of LegC3 has been shown to be associated primarily with the N-terminal domain, which contains coiled-coil sequence motifs. The structure of the N-terminal domain has been determined and it is shown that it is highly alpha-helical and contains a helical bundle followed by a long antiparallel coiled-coil. No similar protein fold has been observed in the PDB. A long loop at the tip of the coiled-coil distal from the membrane is disordered and may be important for interaction with an as yet unidentified protein. | ||
| - | + | Structure of the N-terminal domain of the effector protein LegC3 from Legionella pneumophila.,Yao D, Cherney M, Cygler M Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):436-41. doi:, 10.1107/S139900471302991X. Epub 2014 Jan 29. PMID:24531477<ref>PMID:24531477</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4mu6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] | ||
| + | [[Category: Cherney M]] | ||
| + | [[Category: Cygler M]] | ||
| + | [[Category: Yao D]] | ||
Current revision
Crystal Structure of the N-terminal domain of Effector Protein LegC3 from Legionella pneumophila
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