2axw

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[[Image:2axw.jpg|left|200px]]<br /><applet load="2axw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2axw.jpg|left|200px]]
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caption="2axw, resolution 1.05&Aring;" />
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'''Structure of DraD invasin from uropathogenic Escherichia coli'''<br />
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{{Structure
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|PDB= 2axw |SIZE=350|CAPTION= <scene name='initialview01'>2axw</scene>, resolution 1.05&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE= draD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Structure of DraD invasin from uropathogenic Escherichia coli'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AXW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXW OCA].
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2AXW is a [[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=2AXW OCA].
==Reference==
==Reference==
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Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails., Jedrzejczak R, Dauter Z, Dauter M, Piatek R, Zalewska B, Mroz M, Bury K, Nowicki B, Kur J, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):157-64. Epub 2006, Jan 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16421447 16421447]
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Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails., Jedrzejczak R, Dauter Z, Dauter M, Piatek R, Zalewska B, Mroz M, Bury K, Nowicki B, Kur J, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):157-64. Epub 2006, Jan 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16421447 16421447]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: homodimer]]
[[Category: homodimer]]
[[Category: immunoglobulin-like fold]]
[[Category: immunoglobulin-like fold]]
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[[Category: swapped c-terminal strands]]
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[[Category: swapped c-terminal strand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:55:13 2008''

Revision as of 13:55, 20 March 2008


PDB ID 2axw

Drag the structure with the mouse to rotate
, resolution 1.05Å
Ligands: and
Gene: draD (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

2AXW is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails., Jedrzejczak R, Dauter Z, Dauter M, Piatek R, Zalewska B, Mroz M, Bury K, Nowicki B, Kur J, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):157-64. Epub 2006, Jan 18. PMID:16421447

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