1rxl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1rxl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rxl" /> '''Solution structure of the engineered protein...)
Line 1: Line 1:
-
[[Image:1rxl.gif|left|200px]]<br /><applet load="1rxl" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1rxl.gif|left|200px]]<br /><applet load="1rxl" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rxl" />
caption="1rxl" />
'''Solution structure of the engineered protein Afae-dsc'''<br />
'''Solution structure of the engineered protein Afae-dsc'''<br />
==Overview==
==Overview==
-
Pathogenic bacteria possess adhesion protein complexes that play essential, roles in targeting host cells and in propagating infection. Although each, family of adhesion proteins is generally associated with a specific human, disease, the Dr family from Escherichia coli is a notable exception, as, its members are associated with both diarrheal and urinary tract, infections. These proteins are reported to form both fimbrial and, afimbrial structures at the bacterial cell surface and target a common, host cell receptor, the decay-accelerating factor (DAF or CD55). Using the, newly solved three-dimensional structure of AfaE, we have constructed a, robust atomic resolution model that reveals the structural basis for, assembly by donor strand complementation and for the architecture of, capped surface fibers.
+
Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.
==About this Structure==
==About this Structure==
-
1RXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1RXL OCA].
+
1RXL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1RXL OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Anderson, K.L.]]
+
[[Category: Anderson, K L.]]
-
[[Category: Barlow, P.N.]]
+
[[Category: Barlow, P N.]]
[[Category: Billington, J.]]
[[Category: Billington, J.]]
-
[[Category: Bouguenec, C.Le.]]
+
[[Category: Bouguenec, C Le.]]
-
[[Category: Chen, H.A.]]
+
[[Category: Chen, H A.]]
[[Category: Cota, E]]
[[Category: Cota, E]]
-
[[Category: Lea, S.M.]]
+
[[Category: Lea, S M.]]
[[Category: Matthews, S.]]
[[Category: Matthews, S.]]
-
[[Category: Medof, M.E.]]
+
[[Category: Medof, M E.]]
-
[[Category: Merle, L.du.]]
+
[[Category: Merle, L du.]]
[[Category: Nowicki, B.]]
[[Category: Nowicki, B.]]
[[Category: Pettigrew, D.]]
[[Category: Pettigrew, D.]]
[[Category: Roversi, P.]]
[[Category: Roversi, P.]]
[[Category: Simpson, P.]]
[[Category: Simpson, P.]]
-
[[Category: Smith, R.A.]]
+
[[Category: Smith, R A.]]
[[Category: Urvil, P.]]
[[Category: Urvil, P.]]
[[Category: afae]]
[[Category: afae]]
Line 38: Line 38:
[[Category: upec]]
[[Category: upec]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:56:08 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:55:39 2008''

Revision as of 12:55, 21 February 2008


1rxl

Drag the structure with the mouse to rotate

Solution structure of the engineered protein Afae-dsc

Overview

Pathogenic bacteria possess adhesion protein complexes that play essential roles in targeting host cells and in propagating infection. Although each family of adhesion proteins is generally associated with a specific human disease, the Dr family from Escherichia coli is a notable exception, as its members are associated with both diarrheal and urinary tract infections. These proteins are reported to form both fimbrial and afimbrial structures at the bacterial cell surface and target a common host cell receptor, the decay-accelerating factor (DAF or CD55). Using the newly solved three-dimensional structure of AfaE, we have constructed a robust atomic resolution model that reveals the structural basis for assembly by donor strand complementation and for the architecture of capped surface fibers.

About this Structure

1RXL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

An atomic resolution model for assembly, architecture, and function of the Dr adhesins., Anderson KL, Billington J, Pettigrew D, Cota E, Simpson P, Roversi P, Chen HA, Urvil P, du Merle L, Barlow PN, Medof ME, Smith RA, Nowicki B, Le Bouguenec C, Lea SM, Matthews S, Mol Cell. 2004 Aug 27;15(4):647-57. PMID:15327779

Page seeded by OCA on Thu Feb 21 14:55:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools