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1h6t

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[[Image:1h6t.gif|left|200px]]<br /><applet load="1h6t" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h6t, resolution 1.60&Aring;" />
 
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'''INTERNALIN B: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.'''<br />
 
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==Overview==
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==Internalin B: crystal structure of fused N-terminal domains.==
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Listeria monocytogenes is an opportunistic, food-borne human and animal, pathogen. Host cell invasion requires the action of the internalins A, (InlA) and B (InlB), which are members of a family of listerial, cell-surface proteins. Common to these proteins are three distinctive, N-terminal domains that have been shown to direct host cell-specific, invasion for InlA and InlB. Here, we present the high-resolution crystal, structures of these domains present in InlB and InlH, and show that they, constitute a single "internalin domain". In this internalin domain, a, central LRR region is flanked contiguously by a truncated EF-hand-like cap, and an immunoglobulin (Ig)-like fold. The extended beta-sheet, resulting, from the distinctive fusion of the LRR and the Ig-like folds, constitutes, an adaptable concave interaction surface, which we propose is responsible, for the specific recognition of the host cellular binding partners during, infection.
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<StructureSection load='1h6t' size='340' side='right'caption='[[1h6t]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h6t]] 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=1H6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H6T FirstGlance]. <br>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6t OCA], [https://pdbe.org/1h6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h6t RCSB], [https://www.ebi.ac.uk/pdbsum/1h6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h6t ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/INLB_LISMO INLB_LISMO] Mediates the entry of Listeria monocytogenes into cells.
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== Evolutionary Conservation ==
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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/h6/1h6t_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=1h6t 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 ==
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Listeria monocytogenes is an opportunistic, food-borne human and animal pathogen. Host cell invasion requires the action of the internalins A (InlA) and B (InlB), which are members of a family of listerial cell-surface proteins. Common to these proteins are three distinctive N-terminal domains that have been shown to direct host cell-specific invasion for InlA and InlB. Here, we present the high-resolution crystal structures of these domains present in InlB and InlH, and show that they constitute a single "internalin domain". In this internalin domain, a central LRR region is flanked contiguously by a truncated EF-hand-like cap and an immunoglobulin (Ig)-like fold. The extended beta-sheet, resulting from the distinctive fusion of the LRR and the Ig-like folds, constitutes an adaptable concave interaction surface, which we propose is responsible for the specific recognition of the host cellular binding partners during infection.
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==About this Structure==
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Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain.,Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW J Mol Biol. 2001 Sep 28;312(4):783-94. PMID:11575932<ref>PMID:11575932</ref>
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1H6T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Known structural/functional Site: <scene name='pdbsite=NUL:Aromatic+Residues+On+The+Concave+Face+Of+Inlb+Are+prob.+...'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6T OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain., Schubert WD, Gobel G, Diepholz M, Darji A, Kloer D, Hain T, Chakraborty T, Wehland J, Domann E, Heinz DW, J Mol Biol. 2001 Sep 28;312(4):783-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11575932 11575932]
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</div>
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<div class="pdbe-citations 1h6t" 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]]
[[Category: Listeria monocytogenes]]
[[Category: Listeria monocytogenes]]
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[[Category: Single protein]]
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[[Category: Chakraborty T]]
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[[Category: Chakraborty, T.]]
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[[Category: Darji A]]
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[[Category: Darji, A.]]
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[[Category: Diepholz M]]
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[[Category: Diepholz, M.]]
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[[Category: Domann E]]
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[[Category: Domann, E.]]
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[[Category: Gobel G]]
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[[Category: Gobel, G.]]
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[[Category: Hain T]]
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[[Category: Hain, T.]]
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[[Category: Heinz DW]]
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[[Category: Heinz, D.W.]]
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[[Category: Kloer D]]
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[[Category: Kloer, D.]]
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[[Category: Schubert W-D]]
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[[Category: Schubert, W.D.]]
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[[Category: Wehland J]]
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[[Category: Wehland, J.]]
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[[Category: cell adhesion]]
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[[Category: ef-hand domain]]
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[[Category: ig-like domain]]
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[[Category: leucine rich repeat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:47:07 2008''
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Current revision

Internalin B: crystal structure of fused N-terminal domains.

PDB ID 1h6t

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