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| <StructureSection load='2y5q' size='340' side='right'caption='[[2y5q]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='2y5q' size='340' side='right'caption='[[2y5q]], [[Resolution|resolution]] 3.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2y5q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y5Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2y5q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y5Q FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 3.2Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y5p|2y5p]], [[1h6t|1h6t]], [[2wqw|2wqw]], [[1otm|1otm]], [[2uzx|2uzx]], [[1otn|1otn]], [[2wqv|2wqv]], [[2wqu|2wqu]], [[2uzy|2uzy]], [[1m9s|1m9s]], [[1oto|1oto]], [[2wqx|2wqx]], [[1d0b|1d0b]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2y5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5q OCA], [https://pdbe.org/2y5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y5q RCSB], [https://www.ebi.ac.uk/pdbsum/2y5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y5q ProSAT]</span></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=2y5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5q OCA], [https://pdbe.org/2y5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y5q RCSB], [https://www.ebi.ac.uk/pdbsum/2y5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y5q ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO]] Mediates the entry of Listeria monocytogenes into cells.
| + | [https://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO] Mediates the entry of Listeria monocytogenes into cells. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacterium monocytogenes hominis nyfeldt 1932]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Ebbes, M]] | + | [[Category: Listeria monocytogenes]] |
- | [[Category: Niemann, H H]] | + | [[Category: Ebbes M]] |
- | [[Category: Leucine rich repeat]] | + | [[Category: Niemann HH]] |
- | [[Category: Pathogenicity factor]]
| + | |
- | [[Category: Protein binding]]
| + | |
- | [[Category: Virulence factor]]
| + | |
| Structural highlights
Function
INLB_LISMO Mediates the entry of Listeria monocytogenes into cells.
Publication Abstract from PubMed
Host cell invasion by the facultative intracellular pathogen Listeria monocytogenes requires the invasion protein InlB in many cell types. InlB consists of an N-terminal internalin domain that binds the host cell receptor tyrosine kinase Met and C-terminal GW domains that bind to glycosaminoglycans (GAGs). Met binding and activation is required for host cell invasion, while the interaction between GW domains and GAGs enhances this effect. Soluble InlB elicits the same cellular phenotypes as the natural Met ligand hepatocyte growth factor/scatter factor (HGF/SF), e.g. cell scatter. So far, little is known about the central part of InlB, the B-repeat. Here we present a structural and functional characterization of the InlB B-repeat. The crystal structure reveals a variation of the beta-grasp fold that is most similar to small ubiquitin-like modifiers (SUMOs). However, structural similarity also suggests a potential evolutionary relation to bacterial mucin-binding proteins. The B-repeat defines the prototype structure of a hitherto uncharacterized domain present in over a thousand bacterial proteins. Generally, this domain probably acts as a spacer or a receptor-binding domain in extracellular multi-domain proteins. In cellular assays the B-repeat acts synergistically with the internalin domain conferring to it the ability to stimulate cell motility. Thus, the B-repeat probably binds a further host cell receptor and thereby enhances signaling downstream of Met.
Fold and Function of the InlB B-repeat.,Ebbes M, Bleymuller WM, Cernescu M, Nolker R, Brutschy B, Niemann HH J Biol Chem. 2011 Apr 29;286(17):15496-506. Epub 2011 Feb 23. PMID:21345802[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ebbes M, Bleymuller WM, Cernescu M, Nolker R, Brutschy B, Niemann HH. Fold and Function of the InlB B-repeat. J Biol Chem. 2011 Apr 29;286(17):15496-506. Epub 2011 Feb 23. PMID:21345802 doi:10.1074/jbc.M110.189951
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