7CUS
Crystal structure of the sensor domain of VbrK from Vibrio parahaemolyticus
Summary for 7CUS
| Entry DOI | 10.2210/pdb7cus/pdb |
| Descriptor | DUF3404 domain-containing protein (2 entities in total) |
| Functional Keywords | sensor domain, beta-lactam antibiotic receptor, signaling protein |
| Biological source | Vibrio parahaemolyticus |
| Total number of polymer chains | 1 |
| Total formula weight | 25171.55 |
| Authors | Cho, S.Y.,Yoon, S.I. (deposition date: 2020-08-24, release date: 2020-10-07, Last modification date: 2024-10-23) |
| Primary citation | Cho, S.Y.,Yoon, S.I. Structural analysis of the sensor domain of the beta-lactam antibiotic receptor VbrK from Vibrio parahaemolyticus. Biochem.Biophys.Res.Commun., 533:155-161, 2020 Cited by PubMed Abstract: Bacteria express β-lactamase to counteract the bactericidal effects of β-lactam antibiotics, which are the most widely employed antibacterial drugs. In gram-negative bacteria, the expression of β-lactamase is generally regulated in response to the muropeptide that is generated from the peptidoglycan of the cell wall during β-lactam antibiotic challenge. The direct regulation of β-lactamase expression by β-lactams was recently reported in Vibrio parahaemolyticus, and this regulation is mediated by a two-component regulatory system that consists of the histidine kinase VbrK and the response regulator VbrR. VbrK directly recognizes β-lactam antibiotics using the periplasmic sensor domain (VbrK), a PF11884 Pfam family member, and it delivers the β-lactam signal to VbrR to induce the transcription of the β-lactamase gene. To determine the structural features of VbrK as the prototype of the PF11884 family and provide insights into the β-lactam antibiotic-binding mode of VbrK, we determined the crystal structure of VbrK at 1.65 Å resolution. VbrK folds into a unique curved rod-like structure that has not been previously reported in other families. VbrK consists of two domains (D1 and D2). The D1 domain contains two helix-decorated β-sheets, and the D2 domain adopts a helix-rich structure. VbrK features two terminal disulfide bonds, which would be the canonical property of the PF11884 family. In the VbrK structure, the L82 residue, which was previously shown to play a key role in β-lactam antibiotic recognition, forms a pocket along with its neighboring hydrophobic or positively charged residues. PubMed: 32943185DOI: 10.1016/j.bbrc.2020.09.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
Download full validation report
