PDBsum entry 6gzt

Hydrolase

PDB id: 6gzt

Contents

Protein chain

267 a.a.

Ligands

GOL ×4

SO4

COA

Waters ×147

PDB id:

6gzt

Name:

Hydrolase

Title:

Structure of chlamydia trachomatis effector protein chladub1 bound to coenzyme a

Structure:

Deubiquitinase and deneddylase dub1. Chain: a. Fragment: unp residues 130-401. Synonym: chladub1. Engineered: yes

Source:

Chlamydia trachomatis. Organism_taxid: 813. Gene: cdu1, ctl0247. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.10Å R-factor: 0.184 R-free: 0.216

Authors:

J.N.Pruneda,D.Komander

Key ref:

J.N.Pruneda et al. (2018). A Chlamydia effector combining deubiquitination and acetylation activities induces Golgi fragmentation. Nat Microbiol, 3, 1377-1384. PubMed id: 30397340 DOI: 10.1038/s41564-018-0271-y

Date:

05-Jul-18 Release date: 14-Nov-18

Protein chain

B0B9A0  (CDUB1_CHLT2) -  Deubiquitinase and deneddylase Dub1 from Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)

Seq: 401 a.a.

Struc: 267 a.a.

Enzyme reactions

• Enzyme class: E.C.3.4.22.- - ?????

DOI no: 10.1038/s41564-018-0271-y

Nat Microbiol 3:1377-1384 (2018)

PubMed id: 30397340

A Chlamydia effector combining deubiquitination and acetylation activities induces Golgi fragmentation.

J.N.Pruneda, R.J.Bastidas, E.Bertsoulaki, K.N.Swatek, B.Santhanam, M.J.Clague, R.H.Valdivia, S.Urbé, D.Komander.

ABSTRACT

Pathogenic bacteria are armed with potent effector proteins that subvert host signalling processes during infection¹. The activities of bacterial effectors and their associated roles within the host cell are often poorly understood, particularly for Chlamydia trachomatis², a World Health Organization designated neglected disease pathogen. We identify and explain remarkable dual Lys63-deubiquitinase (DUB) and Lys-acetyltransferase activities in the Chlamydia effector ChlaDUB1. Crystal structures capturing intermediate stages of each reaction reveal how the same catalytic centre of ChlaDUB1 can facilitate such distinct processes, and enable the generation of mutations that uncouple the two activities. Targeted Chlamydia mutant strains allow us to link the DUB activity of ChlaDUB1 and the related, dedicated DUB ChlaDUB2 to fragmentation of the host Golgi apparatus, a key process in Chlamydia infection for which effectors have remained elusive. Our work illustrates the incredible versatility of bacterial effector proteins, and provides important insights towards understanding Chlamydia pathogenesis.