1o9a
From Proteopedia
(New page: 200px<br /> <applet load="1o9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o9a" /> '''SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1...) |
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| - | [[Image:1o9a.gif|left|200px]]<br /> | + | [[Image:1o9a.gif|left|200px]]<br /><applet load="1o9a" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1o9a" size=" | + | |
caption="1o9a" /> | caption="1o9a" /> | ||
'''SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE'''<br /> | '''SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Staphylococcus aureus and Streptococcus pyogenes, two important human | + | Staphylococcus aureus and Streptococcus pyogenes, two important human pathogens, target host fibronectin (Fn) in their adhesion to and invasion of host cells. Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats in an unfolded region of the protein. The bacterium-binding site in the amino-terminal domain (1-5F1) of Fn contains five sequential Fn type 1 (F1) modules. Here we show the structure of a streptococcal (S. dysgalactiae) FnBP peptide (B3) in complex with the module pair 1F12F1. This identifies 1F1- and 2F1-binding motifs in B3 that form additional antiparallel beta-strands on sequential F1 modules-the first example of a tandem beta-zipper. Sequence analyses of larger regions of FnBPs from S. pyogenes and S. aureus reveal a repeating pattern of F1-binding motifs that match the pattern of F1 modules in 1-5F1 of Fn. In the process of Fn-mediated invasion of host cells, therefore, the bacterial proteins seem to exploit the modular structure of Fn by forming extended tandem beta-zippers. This work is a vital step forward in explaining the full mechanism of the integrin-dependent FnBP-mediated invasion of host cells. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O9A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1O9A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Briggs, J | + | [[Category: Briggs, J A.G.]] |
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.]] |
| - | [[Category: Gough, T | + | [[Category: Gough, T S.]] |
[[Category: Gurusiddappa, S.]] | [[Category: Gurusiddappa, S.]] | ||
[[Category: Hook, M.]] | [[Category: Hook, M.]] | ||
| - | [[Category: Kim, J | + | [[Category: Kim, J H.]] |
| - | [[Category: Pickford, A | + | [[Category: Pickford, A R.]] |
| - | [[Category: Pilka, E | + | [[Category: Pilka, E S.]] |
| - | [[Category: Potts, J | + | [[Category: Potts, J R.]] |
[[Category: Schwarz-Linek, U.]] | [[Category: Schwarz-Linek, U.]] | ||
| - | [[Category: Werner, J | + | [[Category: Werner, J M.]] |
[[Category: cell adhesion]] | [[Category: cell adhesion]] | ||
[[Category: fibronectin]] | [[Category: fibronectin]] | ||
[[Category: host-pathogen protein complex]] | [[Category: host-pathogen protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:03 2008'' |
Revision as of 12:15, 21 February 2008
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SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE
Contents |
Overview
Staphylococcus aureus and Streptococcus pyogenes, two important human pathogens, target host fibronectin (Fn) in their adhesion to and invasion of host cells. Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats in an unfolded region of the protein. The bacterium-binding site in the amino-terminal domain (1-5F1) of Fn contains five sequential Fn type 1 (F1) modules. Here we show the structure of a streptococcal (S. dysgalactiae) FnBP peptide (B3) in complex with the module pair 1F12F1. This identifies 1F1- and 2F1-binding motifs in B3 that form additional antiparallel beta-strands on sequential F1 modules-the first example of a tandem beta-zipper. Sequence analyses of larger regions of FnBPs from S. pyogenes and S. aureus reveal a repeating pattern of F1-binding motifs that match the pattern of F1 modules in 1-5F1 of Fn. In the process of Fn-mediated invasion of host cells, therefore, the bacterial proteins seem to exploit the modular structure of Fn by forming extended tandem beta-zippers. This work is a vital step forward in explaining the full mechanism of the integrin-dependent FnBP-mediated invasion of host cells.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
1O9A is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper., Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Hook M, Campbell ID, Potts JR, Nature. 2003 May 8;423(6936):177-81. PMID:12736686
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