1o6t

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[[Image:1o6t.gif|left|200px]]<br /><applet load="1o6t" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1o6t.gif|left|200px]]
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caption="1o6t, resolution 1.60&Aring;" />
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'''INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN,UNCOMPLEXED'''<br />
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{{Structure
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|PDB= 1o6t |SIZE=350|CAPTION= <scene name='initialview01'>1o6t</scene>, resolution 1.60&Aring;
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|SITE= <scene name='pdbsite=AC1:Mes+Binding+Site+For+Chain+A'>AC1</scene>
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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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|ACTIVITY=
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|GENE=
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}}
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'''INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN,UNCOMPLEXED'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1O6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MES:'>MES</scene> and <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Mes+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6T OCA].
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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].
==Reference==
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12526809 12526809]
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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]
[[Category: Listeria monocytogenes]]
[[Category: Listeria monocytogenes]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: leucine rich repeat]]
[[Category: leucine rich repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:34 2008''

Revision as of 11:06, 20 March 2008

Image:1o6t.gif


PDB ID 1o6t

Drag the structure with the mouse to rotate
, resolution 1.60Å
Sites:
Ligands: , , , , and
Coordinates: save as pdb, mmCIF, xml



INTERNALIN (INLA,LISTERIA MONOCYTOGENES)- FUNCTIONAL DOMAIN,UNCOMPLEXED


Overview

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.

About this Structure

1O6T is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.

Reference

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

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