1qun: Difference between revisions

Line 1:

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

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

caption="1qun, resolution 2.8Å" />

'''X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI'''<br />

==Overview==

Type 1 pili-adhesive fibers expressed in most members of the, Enterobacteriaceae family-mediate binding to mannose receptors on host, cells through the FimH adhesin. Pilus biogenesis proceeds by way of the, chaperone/usher pathway. The x-ray structure of the FimC-FimH, chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5, angstrom resolution reveals the basis for carbohydrate recognition and for, pilus assembly. The carboxyl-terminal pilin domain of FimH has an, immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand, complementation mechanism in which the chaperone donates a strand to, complete the pilin domain explains the basis for both chaperone function, and pilus biogenesis.

Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.

==About this Structure==

1QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1QUN OCA].

1QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUN OCA].

==Reference==

Line 14:

[[Category: Protein complex]]

[[Category: Choudhury, D.]]

[[Category: Hultgren, S.J.]]

[[Category: Hultgren, S J.]]

[[Category: Knight, S.]]

[[Category: Langerman, S.]]

Line 22:

[[Category: chaperone adhesin donor strand complementation]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 01:00:~~17 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:56 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1qun.gif|left|200px]]<br /><applet load="1qun" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qun.gif|left|200px]]<br /><applet load="1qun" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qun, resolution 2.8&Aring;" />
 '''X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI'''<br />
 ==Overview==
-Type 1 pili-adhesive fibers expressed in most members of the, Enterobacteriaceae family-mediate binding to mannose receptors on host, cells through the FimH adhesin. Pilus biogenesis proceeds by way of the, chaperone/usher pathway. The x-ray structure of the FimC-FimH, chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5, angstrom resolution reveals the basis for carbohydrate recognition and for, pilus assembly. The carboxyl-terminal pilin domain of FimH has an, immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand, complementation mechanism in which the chaperone donates a strand to, complete the pilin domain explains the basis for both chaperone function, and pilus biogenesis.
+Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.
 ==About this Structure==
-QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QUN OCA].
+QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUN OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Choudhury, D.]]
-[[Category: Hultgren, S.J.]]
+[[Category: Hultgren, S J.]]
 [[Category: Knight, S.]]
 [[Category: Langerman, S.]]
@@ Line 22: / Line 22: @@
 [[Category: chaperone adhesin donor strand complementation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:00:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:56 2008''