3QOU
Crystal Structure of E. coli YbbN
Summary for 3QOU
| Entry DOI | 10.2210/pdb3qou/pdb |
| Descriptor | protein ybbN, CALCIUM ION (3 entities in total) |
| Functional Keywords | thioredoxin-like fold, tetratricopeptide repeat, lysine dimethylation, protein binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 32352.61 |
| Authors | Lin, J.,Wilson, M.A. (deposition date: 2011-02-10, release date: 2011-02-23, Last modification date: 2023-09-13) |
| Primary citation | Lin, J.,Wilson, M.A. Escherichia coli Thioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL. J.Biol.Chem., 286:19459-19469, 2011 Cited by PubMed Abstract: Many proteins contain a thioredoxin (Trx)-like domain fused with one or more partner domains that diversify protein function by the modular construction of new molecules. The Escherichia coli protein YbbN is a Trx-like protein that contains a C-terminal domain with low homology to tetratricopeptide repeat motifs. YbbN has been proposed to act as a chaperone or co-chaperone that aids in heat stress response and DNA synthesis. We report the crystal structure of YbbN, which is an elongated molecule with a mobile Trx domain and four atypical tetratricopeptide repeat motifs. The Trx domain lacks a canonical CXXC active site architecture and is not a functional oxidoreductase. A variety of proteins in E. coli interact with YbbN, including multiple ribosomal protein subunits and a strong interaction with GroEL. YbbN acts as a mild inhibitor of GroESL chaperonin function and ATPase activity, suggesting that it is a negative regulator of the GroESL system. Combined with previous observations that YbbN enhances the DnaK-DnaJ-GrpE chaperone system, we propose that YbbN coordinately regulates the activities of these two prokaryotic chaperones, thereby helping to direct client protein traffic initially to DnaK. Therefore, YbbN may play a role in integrating the activities of different chaperone pathways in E. coli and related bacteria. PubMed: 21498507DOI: 10.1074/jbc.M111.238741 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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