6GZT
Structure of Chlamydia trachomatis effector protein ChlaDUB1 bound to Coenzyme A
Summary for 6GZT
| Entry DOI | 10.2210/pdb6gzt/pdb |
| Descriptor | Deubiquitinase and deneddylase Dub1, GLYCEROL, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | enzyme, ce clan, deubiquitinase, acetyltransferase, hydrolase |
| Biological source | Chlamydia trachomatis |
| Total number of polymer chains | 1 |
| Total formula weight | 32539.22 |
| Authors | Pruneda, J.N.,Komander, D. (deposition date: 2018-07-05, release date: 2018-11-14, Last modification date: 2024-10-16) |
| Primary citation | Pruneda, J.N.,Bastidas, R.J.,Bertsoulaki, E.,Swatek, K.N.,Santhanam, B.,Clague, M.J.,Valdivia, R.H.,Urbe, S.,Komander, D. A Chlamydia effector combining deubiquitination and acetylation activities induces Golgi fragmentation. Nat Microbiol, 3:1377-1384, 2018 Cited by PubMed Abstract: Pathogenic bacteria are armed with potent effector proteins that subvert host signalling processes during infection. The activities of bacterial effectors and their associated roles within the host cell are often poorly understood, particularly for Chlamydia trachomatis, 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. PubMed: 30397340DOI: 10.1038/s41564-018-0271-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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