1h6u: Difference between revisions
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[[Image:1h6u.gif|left|200px]] | [[Image:1h6u.gif|left|200px]] | ||
'''INTERNALIN H: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.''' | {{Structure | ||
|PDB= 1h6u |SIZE=350|CAPTION= <scene name='initialview01'>1h6u</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''INTERNALIN H: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1H6U is a [ | 1H6U 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=1H6U OCA]. | ||
==Reference== | ==Reference== | ||
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:// | 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://www.ncbi.nlm.nih.gov/pubmed/11575932 11575932] | ||
[[Category: Listeria monocytogenes]] | [[Category: Listeria monocytogenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: leucine rich repeat]] | [[Category: leucine rich repeat]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:33:04 2008'' | ||
Revision as of 09:33, 20 March 2008
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INTERNALIN H: CRYSTAL STRUCTURE OF FUSED N-TERMINAL DOMAINS.
Overview
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.
About this Structure
1H6U is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.
Reference
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
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