1otn: Difference between revisions
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==Calcium-binding mutant of the Internalin B LRR domain== | |||
<StructureSection load='1otn' size='340' side='right'caption='[[1otn]], [[Resolution|resolution]] 1.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1otn]] 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=1OTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OTN 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]] 1.97Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1otn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otn OCA], [https://pdbe.org/1otn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1otn RCSB], [https://www.ebi.ac.uk/pdbsum/1otn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1otn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO] Mediates the entry of Listeria monocytogenes into cells. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ot/1otn_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1otn ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Listeria monocytogenes protein InlB promotes invasion of mammalian cells through activation of the receptor tyrosine kinase Met. The InlB N-cap, a approximately 40 residue part of the domain that binds Met, was previously observed to bind two calcium ions in a novel and unusually exposed manner. Because subsequent work raised questions about the existence of these calcium-binding sites, we assayed calcium binding in solution to the InlB N-cap. We show that calcium ions are bound with dissociation constants in the low micromolar range at the two identified sites, and that the sites interact with one another. We demonstrate that the calcium ions are not required for structure, and also find that they have no appreciable effect on Met activation or intracellular invasion. Therefore, our results indicate that the sites are fortuitous in InlB, but also suggest that the simple architecture of the sites may be adaptable for protein engineering purposes. | |||
Characterization of the calcium-binding sites of Listeria monocytogenes InlB.,Marino M, Banerjee M, Copp J, Dramsi S, Chapman T, van der Geer P, Cossart P, Ghosh P Biochem Biophys Res Commun. 2004 Apr 2;316(2):379-86. PMID:15020228<ref>PMID:15020228</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1otn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes]] | [[Category: Listeria monocytogenes]] | ||
[[Category: Chapman | [[Category: Chapman T]] | ||
[[Category: Copp | [[Category: Copp J]] | ||
[[Category: Cossart | [[Category: Cossart P]] | ||
[[Category: Dramsi | [[Category: Dramsi S]] | ||
[[Category: Ghosh P]] | |||
[[Category: Ghosh | [[Category: Marino M]] | ||
[[Category: Marino | [[Category: Van der Geer P]] | ||
[[Category: | |||
Latest revision as of 12:32, 16 August 2023
Calcium-binding mutant of the Internalin B LRR domainCalcium-binding mutant of the Internalin B LRR domain
Structural highlights
FunctionINLB_LISMO Mediates the entry of Listeria monocytogenes into cells. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Listeria monocytogenes protein InlB promotes invasion of mammalian cells through activation of the receptor tyrosine kinase Met. The InlB N-cap, a approximately 40 residue part of the domain that binds Met, was previously observed to bind two calcium ions in a novel and unusually exposed manner. Because subsequent work raised questions about the existence of these calcium-binding sites, we assayed calcium binding in solution to the InlB N-cap. We show that calcium ions are bound with dissociation constants in the low micromolar range at the two identified sites, and that the sites interact with one another. We demonstrate that the calcium ions are not required for structure, and also find that they have no appreciable effect on Met activation or intracellular invasion. Therefore, our results indicate that the sites are fortuitous in InlB, but also suggest that the simple architecture of the sites may be adaptable for protein engineering purposes. Characterization of the calcium-binding sites of Listeria monocytogenes InlB.,Marino M, Banerjee M, Copp J, Dramsi S, Chapman T, van der Geer P, Cossart P, Ghosh P Biochem Biophys Res Commun. 2004 Apr 2;316(2):379-86. PMID:15020228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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