4e7p | pdb_00004e7p

Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the presence of the phosphoryl analog beryllofluoride

spinqualitylabelsall models 4e7p, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4e7p is a 2 chain structure with sequence from Streptococcus pneumoniae R6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.892Å Ligands: BEF, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DNC2_STRR6 Publication Abstract from PubMed Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded alpha/beta fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814(R)) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814(R) was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814(R), resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814. Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride.,Park AK, Moon JH, Lee KS, Chi YM Biochem Biophys Res Commun. 2012 May 4;421(2):403-7. Epub 2012 Apr 10. PMID:22521891 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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