This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7nms
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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='7nms' size='340' side='right'caption='[[7nms]]' scene=''> | + | <StructureSection load='7nms' size='340' side='right'caption='[[7nms]], [[Resolution|resolution]] 1.80Å' 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=7NMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NMS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7nms]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NMS 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=7nms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nms OCA], [https://pdbe.org/7nms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nms RCSB], [https://www.ebi.ac.uk/pdbsum/7nms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nms 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]], [[7pv8|7pv8]], [[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=7nms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nms OCA], [https://pdbe.org/7nms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nms RCSB], [https://www.ebi.ac.uk/pdbsum/7nms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nms 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7nms" 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 07:18, 16 March 2022
InlB392_T332E: T332E variant of Listeria monocytogenes InlB (internalin B) residues 36-392
| |||||||||||
