7LZA
Activated form of VanR from S. coelicolor
Summary for 7LZA
| Entry DOI | 10.2210/pdb7lza/pdb |
| Related | 7LZ9 |
| Descriptor | Putative two-component system response regulator, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | beryllium fluoride, antibiotic resistance, response regulator, transcription |
| Biological source | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Total number of polymer chains | 1 |
| Total formula weight | 25066.58 |
| Authors | Maciunas, L.J.,Loll, P.J. (deposition date: 2021-03-09, release date: 2021-07-14, Last modification date: 2023-10-18) |
| Primary citation | Maciunas, L.J.,Porter, N.,Lee, P.J.,Gupta, K.,Loll, P.J. Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states. Acta Crystallogr D Struct Biol, 77:1027-1039, 2021 Cited by PubMed Abstract: Vancomycin has historically been used as a last-resort treatment for serious bacterial infections. However, vancomycin resistance has become widespread in certain pathogens, presenting a serious threat to public health. Resistance to vancomycin is conferred by a suite of resistance genes, the expression of which is controlled by the VanR-VanS two-component system. VanR is the response regulator in this system; in the presence of vancomycin, VanR accepts a phosphoryl group from VanS, thereby activating VanR as a transcription factor and inducing expression of the resistance genes. This paper presents the X-ray crystal structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states at resolutions of 2.3 and 2.0 Å, respectively. Comparison of the two structures illustrates that phosphorylation of VanR is accompanied by a disorder-to-order transition of helix 4, which lies within the receiver domain of the protein. This transition generates an interface that promotes dimerization of the receiver domain; dimerization in solution was verified using analytical ultracentrifugation. The inactive conformation of the protein does not appear intrinsically unable to bind DNA; rather, it is proposed that in the activated form DNA binding is enhanced by an avidity effect contributed by the receiver-domain dimerization. PubMed: 34342276DOI: 10.1107/S2059798321006288 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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