1p4t

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(New page: 200px<br /><applet load="1p4t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p4t, resolution 2.55&Aring;" /> '''Crystal structure of...)
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[[Image:1p4t.jpg|left|200px]]<br /><applet load="1p4t" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p4t, resolution 2.55&Aring;" />
caption="1p4t, resolution 2.55&Aring;" />
'''Crystal structure of Neisserial surface protein A (NspA)'''<br />
'''Crystal structure of Neisserial surface protein A (NspA)'''<br />
==Overview==
==Overview==
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The neisserial surface protein A (NspA) from Neisseria meningitidis is a, promising vaccine candidate because it is highly conserved among, meningococcal strains and induces bactericidal antibodies. NspA is a, homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution., NspA forms an eight-stranded antiparallel beta-barrel. The four loops at, the extracellular side of the NspA molecule form a long cleft, which, contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic, ligands, such as lipids. In addition, the structure provides a starting, point for structure-based vaccine design.
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The neisserial surface protein A (NspA) from Neisseria meningitidis is a promising vaccine candidate because it is highly conserved among meningococcal strains and induces bactericidal antibodies. NspA is a homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution. NspA forms an eight-stranded antiparallel beta-barrel. The four loops at the extracellular side of the NspA molecule form a long cleft, which contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic ligands, such as lipids. In addition, the structure provides a starting point for structure-based vaccine design.
==About this Structure==
==About this Structure==
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1P4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with SO4, CXE and ETA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P4T OCA].
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1P4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=CXE:'>CXE</scene> and <scene name='pdbligand=ETA:'>ETA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P4T OCA].
==Reference==
==Reference==
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[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bos, M.P.]]
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[[Category: Bos, M P.]]
[[Category: Gros, P.]]
[[Category: Gros, P.]]
[[Category: Tommassen, J.]]
[[Category: Tommassen, J.]]
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[[Category: outer membrane protein]]
[[Category: outer membrane protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:58:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:06 2008''

Revision as of 12:25, 21 February 2008


1p4t, resolution 2.55Å

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Crystal structure of Neisserial surface protein A (NspA)

Overview

The neisserial surface protein A (NspA) from Neisseria meningitidis is a promising vaccine candidate because it is highly conserved among meningococcal strains and induces bactericidal antibodies. NspA is a homolog of the Opa proteins, which mediate adhesion to host cells. Here, we present the crystal structure of NspA, determined to 2.55-A resolution. NspA forms an eight-stranded antiparallel beta-barrel. The four loops at the extracellular side of the NspA molecule form a long cleft, which contains mainly hydrophobic residues and harbors a detergent molecule, suggesting that the protein might function in the binding of hydrophobic ligands, such as lipids. In addition, the structure provides a starting point for structure-based vaccine design.

About this Structure

1P4T is a Single protein structure of sequence from Neisseria meningitidis with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential., Vandeputte-Rutten L, Bos MP, Tommassen J, Gros P, J Biol Chem. 2003 Jul 4;278(27):24825-30. Epub 2003 Apr 26. PMID:12716881

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