2axw: Difference between revisions

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~~'''~~Structure of DraD invasin from uropathogenic Escherichia coli~~'''~~

===Structure of DraD invasin from uropathogenic Escherichia coli===

~~==Overview==~~

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The ~~dra gene cluster of uropathogenic strains of Escherichia coli produces proteins involved in bacterial attachment~~ to ~~and invasion of~~ the ~~eukaryotic host tissues. The crystal structure of a construct of E. coli DraD possessing an additional C-terminal extension of 13 amino acids, including a His6 tag, has been solved~~ at ~~a resolution of 1~~.~~05 angstroms~~. ~~The protein forms symmetric dimers through the exchange of the C-terminal beta-strands~~, ~~which participate in~~ the ~~immunoglobulin~~-~~like beta~~-sandwich fold of each subunit. This structure confirms that DraD is able to act as an acceptor in the donor-strand complementation mechanism of fiber formation but, in contrast to DraE adhesin, its native sequence does not have a donor strand; therefore, DraD can only be located at the tip of the fiber.

The line below this paragraph, {{ABSTRACT_PUBMED_16421447}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16421447 is the PubMed ID number.

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==About this Structure==

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[[Category: Immunoglobulin-like fold]]

[[Category: Swapped c-terminal strand]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 19~~:36:36 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:20:26 2008''

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-[[Image:2axw.jpg|left|200px]]
+{{Seed}}
+[[Image:2axw.png|left|200px]]
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 {{STRUCTURE_2axw|  PDB=2axw  |  SCENE=  }}
-'''Structure of DraD invasin from uropathogenic Escherichia coli'''
+===Structure of DraD invasin from uropathogenic Escherichia coli===
-==Overview==
+<!--
-The dra gene cluster of uropathogenic strains of Escherichia coli produces proteins involved in bacterial attachment to and invasion of the eukaryotic host tissues. The crystal structure of a construct of E. coli DraD possessing an additional C-terminal extension of 13 amino acids, including a His6 tag, has been solved at a resolution of 1.05 angstroms. The protein forms symmetric dimers through the exchange of the C-terminal beta-strands, which participate in the immunoglobulin-like beta-sandwich fold of each subunit. This structure confirms that DraD is able to act as an acceptor in the donor-strand complementation mechanism of fiber formation but, in contrast to DraE adhesin, its native sequence does not have a donor strand; therefore, DraD can only be located at the tip of the fiber.
+The line below this paragraph, {{ABSTRACT_PUBMED_16421447}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16421447 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16421447}}
 ==About this Structure==
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 [[Category: Immunoglobulin-like fold]]
 [[Category: Swapped c-terminal strand]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:36:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:20:26 2008''