View source for 7pv8


==InlB392_T332E: T332E variant of Listeria monocytogenes InlB (internalin B) residues 36-392==
<StructureSection load='7pv8' size='340' side='right'caption='[[7pv8]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pv8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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='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>
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pv8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria monocytogenes EGD-e]]
[[Category: Geerds C]]
[[Category: Niemann HH]]