2rnj | pdb_00002rnj

NMR Structure of The S. Aureus VraR DNA Binding Domain

spinqualitylabelsall models 2rnj, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rnj is a 1 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: vraR ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VRAR_STAAM] Member of the two-component regulatory system VraS/VraR involved in the control of the cell wall peptidoglycan biosynthesis. VraR is overexpressed in strain Mu50, which leads to vancomycin resistance. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed In Staphylococcus aureus, a two-component signaling system consisting of the histidine kinase VraS and the response regulator VraR stimulates gene expression in response to antibiotics that inhibit cell wall formation. With respect to understanding the mechanism of the VraSR response and precise interaction of VraR at promoter sites, the structure of the VraR DNA binding domain (DBD) was determined using NMR methods. The DBD demonstrates a four-helix configuration that is shared with the NarL/FixJ family of response regulators and is monomeric in solution. Unobservable amide resonances in VraR NMR spectra coincided with a set of DNA backbone contact sites predicted from a model of a VraR-DNA complex. This observation suggests that a degree of conformational sampling is required to achieve a high-affinity interaction with DNA. On the basis of chemical shift differences and line broadening, an amino-terminal 3 10 helix and a portion of helix H4 identify a continuous surface that may link the DBD to the receiver domain. The full-length VraR protein thermally denatured with a single transition, suggesting that the receiver domain and DBD were integrated and not simply tethered. Of note, the DBD alone denatured at a temperature that was 21 degrees C higher than that of the full-length protein. Thus, the DBD appears to be thermodynamically and structurally sensitive to state of the receiver domain. The NMR Structure of the Staphylococcus aureus Response Regulator VraR DNA Binding Domain Reveals a Dynamic Relationship between It and Its Associated Receiver Domain.,Donaldson LW Biochemistry. 2008 Mar 18;47(11):3379-88. Epub 2008 Feb 23. PMID:18293926 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Response regulator

Proteopedia Page Contributors and Editors (what is this?)

OCA