4l3a
From Proteopedia
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| - | + | ==Crystal structure of Internalin K (InlK) from Listeria monocytogenes== | |
| - | + | <StructureSection load='4l3a' size='340' side='right' caption='[[4l3a]], [[Resolution|resolution]] 2.59Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4l3a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L3A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L3A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l3f|4l3f]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmo1290 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</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=4l3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l3a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l3a RCSB], [http://www.ebi.ac.uk/pdbsum/4l3a PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Listeria monocytogenes is a human pathogen that employs a wide variety of virulence factors in order to adhere to, invade, and replicate within target cells. Internalins play key roles in processes ranging from adhesion to receptor recognition and are thus essential for infection. Recently, InlK, a surface-associated internalin, was shown to be involved in Listeria's ability to escape from autophagy by recruitment of the major vault protein (MVP) to the bacterial surface. Here, we report the structure of InlK, which harbors four domains arranged in the shape of a "bent arm". The structure supports a role for the "elbow" of InlK in partner recognition, as well as of two Ig-like pedestals intercalated by hinge regions in the projection of InlK away from the surface of the bacterium. The unusual fold and flexibility of InlK could be essential for MVP binding and concealment from recognition by molecules involved in the autophagic process. | ||
| - | + | Structure of Internalin InlK from the Human Pathogen Listeriamonocytogenes.,Neves D, Job V, Dortet L, Cossart P, Dessen A J Mol Biol. 2013 Aug 16. pii: S0022-2836(13)00513-5. doi:, 10.1016/j.jmb.2013.08.010. PMID:23958637<ref>PMID:23958637</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Lismo]] | [[Category: Lismo]] | ||
| - | [[Category: Neves, D | + | [[Category: Neves, D]] |
[[Category: Cell invasion]] | [[Category: Cell invasion]] | ||
[[Category: Immune system evasion]] | [[Category: Immune system evasion]] | ||
[[Category: Leucine rich repeat]] | [[Category: Leucine rich repeat]] | ||
[[Category: Major vault protein]] | [[Category: Major vault protein]] | ||
Revision as of 07:26, 15 February 2015
Crystal structure of Internalin K (InlK) from Listeria monocytogenes
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