5B5Q

1.7 Angstroms structure of ChlaDub1 from Chlamydia Trachomatis

Summary for 5B5Q

• Entry DOI: 10.2210/pdb5b5q/pdb
• Descriptor: Membrane thiol protease, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: chlamydia trachomatis, deubiquitinase., hydrolase
• Biological source: Chlamydia trachomatis; More
• Total number of polymer chains: 2
• Total formula weight: 56337.74

Authors

Ramirez, Y.A.,Kisker, C.,Sauer, F. (deposition date: 2016-05-13, release date: 2017-03-29, Last modification date: 2024-03-20)

Primary citation

Fischer, A.,Harrison, K.S.,Ramirez, Y.,Auer, D.,Chowdhury, S.R.,Prusty, B.K.,Sauer, F.,Dimond, Z.,Kisker, C.,Scott Hefty, P.,Rudel, T.
Chlamydia trachomatis-containing vacuole serves as deubiquitination platform to stabilize Mcl-1 and to interfere with host defense
Elife, 6:-, 2017

PubMed Abstract: Obligate intracellular replicate in a membrane-bound vacuole called inclusion, which serves as a signaling interface with the host cell. Here, we show that the chlamydial deubiquitinating enzyme (Cdu) 1 localizes in the inclusion membrane and faces the cytosol with the active deubiquitinating enzyme domain. The structure of this domain revealed high similarity to mammalian deubiquitinases with a unique α-helix close to the substrate-binding pocket. We identified the apoptosis regulator Mcl-1 as a target that interacts with Cdu1 and is stabilized by deubiquitination at the chlamydial inclusion. A chlamydial transposon insertion mutant in the Cdu1-encoding gene exhibited increased Mcl-1 and inclusion ubiquitination and reduced Mcl-1 stabilization. Additionally, inactivation of Cdu1 led to increased sensitivity of for IFNγ and impaired infection in mice. Thus, the chlamydial inclusion serves as an enriched site for a deubiquitinating activity exerting a function in selective stabilization of host proteins and protection from host defense.

PubMed: 28347402
DOI: 10.7554/eLife.21465

Experimental method

X-RAY DIFFRACTION (1.7 Å)