PDBsum entry 6gzs

Hydrolase

PDB id: 6gzs

Contents

Protein chains

250 a.a.

75 a.a.

Ligands

GOL

SO4

AYE

Waters ×184

PDB id:

6gzs

Name:

Hydrolase

Title:

Structure of chlamydia trachomatis effector protein chladub1 bound to ubiquitin

Structure:

Deubiquitinase and deneddylase dub1. Chain: a. Synonym: chladub1. Engineered: yes. Polyubiquitin-b. Chain: b. Engineered: yes

Source:

Chlamydia trachomatis serovar l2 (strain 434/bu / atcc vr-902b). Organism_taxid: 471472. Strain: 434/bu / atcc vr-902b. Gene: cdu1, ctl0247. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human.

Resolution:

1.90Å R-factor: 0.183 R-free: 0.213

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: 250 a.a.

Protein chain

P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens

Seq: 229 a.a.

Struc: 75 a.a.

Enzyme reactions

• Enzyme class: Chain A: 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.