1oqv: Difference between revisions

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[[Image:1oqv.jpg|left|200px]]<br /><applet load="1oqv" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1oqv.jpg|left|200px]]<br /><applet load="1oqv" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1oqv, resolution 1.3Å" />

'''Structure of TcpA, the Type IV pilin subunit from the toxin co-regulated pilus of Vibrio cholerae classical biotype'''<br />

==Overview==

Pilin assembly into type IV pili is required for virulence by bacterial, pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and, meningitis. Crystal structures of soluble, N-terminally truncated pilin, from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK, pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared, architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the, structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the, extended hydrophobic alpha helices make multisubunit contacts to provide, mechanical strength and flexibility. Outside, distinct interactions of, adaptable heads contribute surface variation for specificity of pilus, function in antigenicity, motility, adhesion, and colony formation.

Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.

==About this Structure==

1OQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA].

1OQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA].

==Reference==

Line 14:

[[Category: Vibrio cholerae]]

[[Category: Craig, L.]]

[[Category: Tainer, J.A.]]

[[Category: Tainer, J A.]]

[[Category: GOL]]

[[Category: adhesin]]

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[[Category: vibrio cholerae]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov~~ 20 ~~23:06~~:~~55 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:43 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1oqv.jpg|left|200px]]<br /><applet load="1oqv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1oqv.jpg|left|200px]]<br /><applet load="1oqv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1oqv, resolution 1.3&Aring;" />
 '''Structure of TcpA, the Type IV pilin subunit from the toxin co-regulated pilus of Vibrio cholerae classical biotype'''<br />
 ==Overview==
-Pilin assembly into type IV pili is required for virulence by bacterial, pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and, meningitis. Crystal structures of soluble, N-terminally truncated pilin, from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK, pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared, architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the, structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the, extended hydrophobic alpha helices make multisubunit contacts to provide, mechanical strength and flexibility. Outside, distinct interactions of, adaptable heads contribute surface variation for specificity of pilus, function in antigenicity, motility, adhesion, and colony formation.
+Pilin assembly into type IV pili is required for virulence by bacterial pathogens that cause diseases such as cholera, pneumonia, gonorrhea, and meningitis. Crystal structures of soluble, N-terminally truncated pilin from Vibrio cholera toxin-coregulated pilus (TCP) and full-length PAK pilin from Pseudomonas aeruginosa reveal a novel TCP fold, yet a shared architecture for the type IV pilins. In each pilin subunit a conserved, extended, N-terminal alpha helix wrapped by beta strands anchors the structurally variable globular head. Inside the assembled pilus, characterized by cryo-electron microscopy and crystallography, the extended hydrophobic alpha helices make multisubunit contacts to provide mechanical strength and flexibility. Outside, distinct interactions of adaptable heads contribute surface variation for specificity of pilus function in antigenicity, motility, adhesion, and colony formation.
 ==About this Structure==
-OQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA].
+OQV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQV OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Vibrio cholerae]]
 [[Category: Craig, L.]]
-[[Category: Tainer, J.A.]]
+[[Category: Tainer, J A.]]
 [[Category: GOL]]
 [[Category: adhesin]]
@@ Line 25: / Line 25: @@
 [[Category: vibrio cholerae]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:06:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:43 2008''