1o6t

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[[Image:1o6t.gif|left|200px]]
 
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{{Structure
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==Internalin (INLA, Listeria monocytogenes) - functional domain, uncomplexed==
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|PDB= 1o6t |SIZE=350|CAPTION= <scene name='initialview01'>1o6t</scene>, resolution 1.60&Aring;
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<StructureSection load='1o6t' size='340' side='right'caption='[[1o6t]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Mes+Binding+Site+For+Chain+A'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene> and <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene>
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<table><tr><td colspan='2'>[[1o6t]] 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=1O6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6T FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6t OCA], [https://pdbe.org/1o6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6t RCSB], [https://www.ebi.ac.uk/pdbsum/1o6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6t ProSAT]</span></td></tr>
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</table>
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'''INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN,UNCOMPLEXED'''
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== Function ==
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[https://www.uniprot.org/uniprot/INLA_LISMO INLA_LISMO] Mediates the entry of L.monocytogenes into cells.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/1o6t_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1o6t ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.
Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.
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==About this Structure==
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Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.,Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW Cell. 2002 Dec 13;111(6):825-36. PMID:12526809<ref>PMID:12526809</ref>
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1O6T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6T OCA].
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==Reference==
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Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin., Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW, Cell. 2002 Dec 13;111(6):825-36. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12526809 12526809]
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[[Category: Listeria monocytogenes]]
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[[Category: Single protein]]
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[[Category: Beier, V.]]
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[[Category: Chakraborty, T.]]
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[[Category: Domann, E.]]
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[[Category: Heinz, D W.]]
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[[Category: Machner, M.]]
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[[Category: Schubert, W D.]]
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[[Category: Urbanke, C.]]
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[[Category: Wehland, J.]]
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[[Category: Ziehm, T.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: MES]]
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[[Category: MG]]
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[[Category: SO4]]
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[[Category: bacterial infection]]
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[[Category: cell adhesion]]
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[[Category: cell-wall surface protein]]
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[[Category: leucine rich repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:34 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1o6t" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Listeria monocytogenes EGD-e]]
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[[Category: Beier V]]
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[[Category: Chakraborty T]]
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[[Category: Domann E]]
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[[Category: Heinz DW]]
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[[Category: Machner MP]]
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[[Category: Schubert W-D]]
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[[Category: Urbanke C]]
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[[Category: Wehland J]]
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[[Category: Ziehm T]]

Current revision

Internalin (INLA, Listeria monocytogenes) - functional domain, uncomplexed

PDB ID 1o6t

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