2axw: Difference between revisions

Line 4:

==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 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.

==About this Structure==

Line 29:

[[Category: swapped c-terminal strands]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Tue Jan 29 18~~:12:29 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:07 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==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 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.
 ==About this Structure==
@@ Line 29: / Line 29: @@
 [[Category: swapped c-terminal strands]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:12:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:07 2008''