7PQ7

Crystal structure of Campylobacter jejuni DsbA1

Summary for 7PQ7

• Entry DOI: 10.2210/pdb7pq7/pdb
• Descriptor: Thiol:disulfide interchange protein DsbA, TRIETHYLENE GLYCOL, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: periplasmic, disulfide bond, thioredoxin fold, posttranslational modification, oxidoreductase
• Biological source: Campylobacter jejuni
• Total number of polymer chains: 2
• Total formula weight: 47137.12

Authors

Wilk, P.,Orlikowska, M.,Banas, A.M.,Bocian-Ostrzycka, K.M.,Jagusztyn-Krynicka, E.K. (deposition date: 2021-09-16, release date: 2021-12-29, Last modification date: 2024-01-31)

Primary citation

Banas, A.M.,Bocian-Ostrzycka, K.M.,Dunin-Horkawicz, S.,Ludwiczak, J.,Wilk, P.,Orlikowska, M.,Wyszynska, A.,Dabrowska, M.,Plichta, M.,Spodzieja, M.,Polanska, M.A.,Malinowska, A.,Jagusztyn-Krynicka, E.K.
Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases of Campylobacter jejuni and Their Impact on Bacterial Physiology and Pathogenesis.
Int J Mol Sci, 22:-, 2021

PubMed Abstract: The bacterial proteins of the Dsb family catalyze the formation of disulfide bridges between cysteine residues that stabilize protein structures and ensure their proper functioning. Here, we report the detailed analysis of the Dsb pathway of . The oxidizing Dsb system of this pathogen is unique because it consists of two monomeric DsbAs (DsbA1 and DsbA2) and one dimeric bifunctional protein (C8J_1298). Previously, we showed that DsbA1 and C8J_1298 are redundant. Here, we unraveled the interaction between the two monomeric DsbAs by in vitro and in vivo experiments and by solving their structures and found that both monomeric DsbAs are dispensable proteins. Their structures confirmed that they are homologs of EcDsbL. The slight differences seen in the surface charge of the proteins do not affect the interaction with their redox partner. Comparative proteomics showed that several respiratory proteins, as well as periplasmic transport proteins, are targets of the Dsb system. Some of these, both donors and electron acceptors, are essential elements of the respiratory process under oxygen-limiting conditions in the host intestine. The data presented provide detailed information on the function of the Dsb system, identifying it as a potential target for novel antibacterial molecules.

PubMed: 34948248
DOI: 10.3390/ijms222413451

Experimental method

X-RAY DIFFRACTION (1.55 Å)