1RCW

Crystal structure of CT610 from Chlamydia trachomatis

Summary for 1RCW

• Entry DOI: 10.2210/pdb1rcw/pdb
• Descriptor: CT610, FE (III) ION (3 entities in total)
• Functional Keywords: iron, di-iron, redox enzyme, metallo enzyme, oxidoreductase, toxin
• Biological source: Chlamydia trachomatis
• Cellular location: Secreted: O84616
• Total number of polymer chains: 3
• Total formula weight: 81196.46

Authors

Schwarzenbacher, R.,Liddington, R.C. (deposition date: 2003-11-04, release date: 2004-05-04, Last modification date: 2024-11-20)

Primary citation

Schwarzenbacher, R.,Stenner-Liewen, F.,Liewen, H.,Robinson, H.,Yuan, H.,Bossy-Wetzel, E.,Reed, J.C.,Liddington, R.C.
Structure of the Chlamydia protein CADD reveals a redox enzyme that modulates host cell apoptosis.
J.Biol.Chem., 279:29320-29324, 2004

PubMed Abstract: 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.

PubMed: 15087448
DOI: 10.1074/jbc.M401268200

Experimental method

X-RAY DIFFRACTION (2.5 Å)