6A07
Salmonella Typhi YfdX in the F222 space group at 1.5 A resolution
Summary for 6A07
| Entry DOI | 10.2210/pdb6a07/pdb |
| Descriptor | YfdX protein, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | sty3178, yfdx, salmonella, unknown function |
| Biological source | Salmonella enterica I |
| Total number of polymer chains | 1 |
| Total formula weight | 20794.92 |
| Authors | |
| Primary citation | Lee, H.S.,Lee, S.,Kim, J.S.,Lee, H.R.,Shin, H.C.,Lee, M.S.,Jin, K.S.,Kim, C.H.,Ku, B.,Ryu, C.M.,Kim, S.J. Structural and Physiological Exploration ofSalmonellaTyphi YfdX Uncovers Its Dual Function in Bacterial Antibiotic Stress and Virulence. Front Microbiol, 9:3329-3329, 2018 Cited by PubMed Abstract: YfdX is a prokaryotic protein encoded by several pathogenic bacteria including serovar Typhi, which causes one of the most fatal infectious diseases, typhoid fever. YfdX is a product of the operon and is known to be under the control of EvgA, a regulator protein controlling the expression of several proteins involved in response to environmental stress, in . Nevertheless, unlike other proteins encoded by the same operon, the structural and physiological aspects of YfdX have been poorly characterized. Here, we identified a previously unknown pH-dependent stoichiometric conversion of . Typhi YfdX between dimeric and tetrameric states; this conversion was further analyzed via determining its structure by X-ray crystallography at high resolution and by small-angle X-ray scattering in a solution state and via structure-based mutant studies. Biologically, YfdX was proven to be critically involved in susceptibility to two β-lactam antibiotics, penicillin G and carbenicillin, as bacterial growth significantly impaired by its deficiency upon treatment with each of the two antibiotics was recovered by chromosomal complementation. Furthermore, by using larvae as an model of infection, we demonstrated that virulence was remarkably enhanced by YfdX deficiency, which was complemented by a transient expression of the wild-type or dimeric mutant but not by that of the monomeric mutant. The present study work provides direct evidence regarding the participation of YfdX in antibiotic susceptibility and in the modulation of bacterial virulence, providing a new insight into this pathogen's strategies for survival and growth. PubMed: 30692978DOI: 10.3389/fmicb.2018.03329 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.501 Å) |
Structure validation
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