7pv8
From Proteopedia
(Difference between revisions)
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==InlB392_T332E: T332E variant of Listeria monocytogenes InlB (internalin B) residues 36-392== | ==InlB392_T332E: T332E variant of Listeria monocytogenes InlB (internalin B) residues 36-392== | ||
| - | <StructureSection load='7pv8' size='340' side='right'caption='[[7pv8]]' scene=''> | + | <StructureSection load='7pv8' size='340' side='right'caption='[[7pv8]], [[Resolution|resolution]] 2.05Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PV8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7pv8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PV8 FirstGlance]. <br> |
| - | </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=7pv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pv8 OCA], [https://pdbe.org/7pv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pv8 RCSB], [https://www.ebi.ac.uk/pdbsum/7pv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pv8 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d0b|1d0b]], [[1h6t|1h6t]], [[1m9s|1m9s]], [[2y5p|2y5p]], [[2y5q|2y5q]], [[7nms|7nms]], [[7pv9|7pv9]]</div></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=7pv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pv8 OCA], [https://pdbe.org/7pv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pv8 RCSB], [https://www.ebi.ac.uk/pdbsum/7pv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pv8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO]] Mediates the entry of Listeria monocytogenes into cells. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | InlB, a bacterial agonist of the human receptor tyrosine kinase MET, consists of an N-terminal internalin domain, a central B repeat and three C-terminal GW domains. In all previous structures of full-length InlB or an InlB construct lacking the GW domains (InlB392), there was no interpretable electron density for the B repeat. Here, three InlB392 crystal structures in which the B repeat is resolved are described. These are the first structures to reveal the relative orientation of the internalin domain and the B repeat. A wild-type structure and two structures of the T332E variant together contain five crystallographically independent molecules. Surprisingly, the threonine-to-glutamate substitution in the B repeat substantially improved the crystallization propensity and crystal quality of the T332E variant. The internalin domain and B repeat are quite rigid internally, but are flexibly linked to each other. The new structures show that inter-domain flexibility is the most likely cause of the missing electron density for the B repeat in previous InlB structures. A potential binding groove between B-repeat strand beta2 and an adjacent loop forms an important crystal contact in all five crystallographically independent chains. This region may represent a hydrophobic `sticky patch' that supports protein-protein interactions. This assumption agrees with the previous finding that all known inactivating point mutations in the B repeat lie within strand beta2. The groove formed by strand beta2 and the adjacent loop may thus represent a functionally important protein-protein interaction site in the B repeat. | ||
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| + | A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat.,Geerds C, Bleymuller WM, Meyer T, Widmann C, Niemann HH Acta Crystallogr D Struct Biol. 2022 Mar 1;78(Pt 3):310-320. doi:, 10.1107/S2059798322000432. Epub 2022 Feb 18. PMID:35234145<ref>PMID:35234145</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7pv8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Geerds C]] | + | [[Category: Geerds, C]] |
| - | [[Category: Niemann | + | [[Category: Niemann, H H]] |
| + | [[Category: Cell invasion]] | ||
| + | [[Category: Leucine rich repeat]] | ||
| + | [[Category: Pathogenicity]] | ||
| + | [[Category: Protein binding]] | ||
| + | [[Category: Virulence factor]] | ||
Revision as of 07:19, 16 March 2022
InlB392_T332E: T332E variant of Listeria monocytogenes InlB (internalin B) residues 36-392
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