title: Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region.
abstract: Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3(-)) was determined at 2.0 Å. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the α4-β5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.
authors.affiliation: Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, South Korea; Division of Polar Life Sciences, Korea Polar Research Institute, Yeonsu-gu, Incheon 406-840, South Korea.
authors.forename: Ae Kyung
authors.initials: AK
authors.lastname: Park
authors.affiliation: Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, South Korea.
authors.forename: Jeong Hye
authors.initials: JH
authors.lastname: Lee
authors.affiliation: Division of Biotechnology, College of Life Sciences, Korea University, Seoul 136-713, South Korea. Electronic address: ezeg@korea.ac.kr.
authors.forename: Young Min
authors.initials: YM
authors.lastname: Chi
authors.affiliation: Division of Polar Life Sciences, Korea Polar Research Institute, Yeonsu-gu, Incheon 406-840, South Korea. Electronic address: hpark@kopri.re.kr.
authors.forename: Hyun
authors.initials: H
authors.lastname: Park
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001608:Beryllium / Q000378:metabolism; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D005459:Fluorides / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D010710:Phosphates / Q000378:metabolism*; D010766:Phosphorylation; D011008:Pneumococcal Infections / Q000382:microbiology; D011487:Protein Conformation; D055503:Protein Multimerization; D013296:Streptococcus pneumoniae / Q000737:chemistry* / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D010710:Phosphates; C035982:beryllium fluoride; D001608:Beryllium; D005459:Fluorides
keywords: NarL subfamily; Phosphorylation; Response regulator; Streptococcus pneumoniae; Two-component system