1rcw
From Proteopedia
(New page: 200px<br /><applet load="1rcw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rcw, resolution 2.50Å" /> '''Crystal structure of...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1rcw.jpg|left|200px]]<br /><applet load="1rcw" size=" | + | [[Image:1rcw.jpg|left|200px]]<br /><applet load="1rcw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rcw, resolution 2.50Å" /> | caption="1rcw, resolution 2.50Å" /> | ||
'''Crystal structure of CT610 from Chlamydia trachomatis'''<br /> | '''Crystal structure of CT610 from Chlamydia trachomatis'''<br /> | ||
==Overview== | ==Overview== | ||
- | The Chlamydia protein CADD (Chlamydia protein associating with death | + | The Chlamydia protein CADD (Chlamydia protein associating with death domains) has been implicated in the modulation of host cell apoptosis via binding to the death domains of tumor necrosis factor family receptors. Transfection of CADD into mammalian cells induces apoptosis. Here we present the CADD crystal structure, which reveals a dimer of seven-helix bundles. Each bundle contains a di-iron center adjacent to an internal cavity, forming an active site similar to that of methane mono-oxygenase hydrolase. We further show that CADD mutants lacking critical metal-coordinating residues are substantially less effective in inducing apoptosis but retain their ability to bind to death domains. We conclude that CADD is a novel redox protein toxin unique to Chlamydia species and propose that both its redox activity and death domain binding ability are required for its biological activity. |
==About this Structure== | ==About this Structure== | ||
- | 1RCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1RCW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydia_trachomatis Chlamydia trachomatis] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCW OCA]. |
==Reference== | ==Reference== | ||
Line 13: | Line 13: | ||
[[Category: Chlamydia trachomatis]] | [[Category: Chlamydia trachomatis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Liddington, R | + | [[Category: Liddington, R C.]] |
[[Category: Schwarzenbacher, R.]] | [[Category: Schwarzenbacher, R.]] | ||
[[Category: FE]] | [[Category: FE]] | ||
Line 21: | Line 21: | ||
[[Category: redox enzyme]] | [[Category: redox enzyme]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:32 2008'' |
Revision as of 12:49, 21 February 2008
|
Crystal structure of CT610 from Chlamydia trachomatis
Overview
The Chlamydia protein CADD (Chlamydia protein associating with death domains) has been implicated in the modulation of host cell apoptosis via binding to the death domains of tumor necrosis factor family receptors. Transfection of CADD into mammalian cells induces apoptosis. Here we present the CADD crystal structure, which reveals a dimer of seven-helix bundles. Each bundle contains a di-iron center adjacent to an internal cavity, forming an active site similar to that of methane mono-oxygenase hydrolase. We further show that CADD mutants lacking critical metal-coordinating residues are substantially less effective in inducing apoptosis but retain their ability to bind to death domains. We conclude that CADD is a novel redox protein toxin unique to Chlamydia species and propose that both its redox activity and death domain binding ability are required for its biological activity.
About this Structure
1RCW is a Single protein structure of sequence from Chlamydia trachomatis with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the Chlamydia protein CADD reveals a redox enzyme that modulates host cell apoptosis., Schwarzenbacher R, Stenner-Liewen F, Liewen H, Robinson H, Yuan H, Bossy-Wetzel E, Reed JC, Liddington RC, J Biol Chem. 2004 Jul 9;279(28):29320-4. Epub 2004 Apr 15. PMID:15087448
Page seeded by OCA on Thu Feb 21 14:49:32 2008