7lza | pdb_00007lza

Activated form of VanR from S. coelicolor

spinqualitylabelsall models 7lza, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7lza is a 1 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.03Å Ligands: BEF, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8CJW1_STRCO Publication Abstract from PubMed 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 A, 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. Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.,Maciunas LJ, Porter N, Lee PJ, Gupta K, Loll PJ Acta Crystallogr D Struct Biol. 2021 Aug 1;77(Pt 8):1027-1039. doi:, 10.1107/S2059798321006288. Epub 2021 Jul 29. PMID:34342276 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lysozyme 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA