1q5f

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(New page: 200px<br /><applet load="1q5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q5f" /> '''NMR Structure of Type IVb pilin (PilS) from ...)
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'''NMR Structure of Type IVb pilin (PilS) from Salmonella typhi'''<br />
'''NMR Structure of Type IVb pilin (PilS) from Salmonella typhi'''<br />
==Overview==
==Overview==
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The structure of the N-terminal-truncated Type IVb structural pilin, (t-PilS) from Salmonella typhi was determined by NMR. Although, topologically similar to the recently determined x-ray structure of pilin, from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with, known structure, t-PilS contains many distinct structural features. The, protein contains an extra pair of beta-strands in the N-terminal alphabeta, loop that align with the major beta-strands to form a continuous, 7-stranded antiparallel beta-sheet. The C-terminal disulfide-bonded region, of t-PilS is only half the length of that of toxin-coregulated pilus, pilin. A model of S. typhi pilus has been proposed and mutagenesis studies, suggested that residues on both the alphabeta loop and the C-terminal, disulfide-bonded region of PilS might be involved in binding specificity, of the pilus. This model structure reveals an exposed surface between, adjacent subunits of PilS that could be a potential binding site for the, cystic fibrosis transmembrane conductance regulator.
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The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with known structure, t-PilS contains many distinct structural features. The protein contains an extra pair of beta-strands in the N-terminal alphabeta loop that align with the major beta-strands to form a continuous 7-stranded antiparallel beta-sheet. The C-terminal disulfide-bonded region of t-PilS is only half the length of that of toxin-coregulated pilus pilin. A model of S. typhi pilus has been proposed and mutagenesis studies suggested that residues on both the alphabeta loop and the C-terminal disulfide-bonded region of PilS might be involved in binding specificity of the pilus. This model structure reveals an exposed surface between adjacent subunits of PilS that could be a potential binding site for the cystic fibrosis transmembrane conductance regulator.
==About this Structure==
==About this Structure==
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1Q5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhi Salmonella typhi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q5F OCA].
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1Q5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhi Salmonella typhi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5F OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hackett, J.]]
[[Category: Hackett, J.]]
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[[Category: Mok, Y.K.]]
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[[Category: Mok, Y K.]]
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[[Category: Tan, Y.W.]]
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[[Category: Tan, Y W.]]
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[[Category: Xu, X.F.]]
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[[Category: Xu, X F.]]
[[Category: Zhang, M.]]
[[Category: Zhang, M.]]
[[Category: alpha-beta roll]]
[[Category: alpha-beta roll]]
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[[Category: type ivb pilin]]
[[Category: type ivb pilin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:36:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:36:01 2008''

Revision as of 12:36, 21 February 2008


1q5f

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NMR Structure of Type IVb pilin (PilS) from Salmonella typhi

Overview

The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with known structure, t-PilS contains many distinct structural features. The protein contains an extra pair of beta-strands in the N-terminal alphabeta loop that align with the major beta-strands to form a continuous 7-stranded antiparallel beta-sheet. The C-terminal disulfide-bonded region of t-PilS is only half the length of that of toxin-coregulated pilus pilin. A model of S. typhi pilus has been proposed and mutagenesis studies suggested that residues on both the alphabeta loop and the C-terminal disulfide-bonded region of PilS might be involved in binding specificity of the pilus. This model structure reveals an exposed surface between adjacent subunits of PilS that could be a potential binding site for the cystic fibrosis transmembrane conductance regulator.

About this Structure

1Q5F is a Single protein structure of sequence from Salmonella typhi. Full crystallographic information is available from OCA.

Reference

NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus., Xu XF, Tan YW, Lam L, Hackett J, Zhang M, Mok YK, J Biol Chem. 2004 Jul 23;279(30):31599-605. Epub 2004 May 24. PMID:15159389

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