4ZMR

Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region

Summary for 4ZMR

• Entry DOI: 10.2210/pdb4zmr/pdb
• Related: 4zms
• Descriptor: Response regulator, MAGNESIUM ION, BERYLLIUM TRIFLUORIDE ION, ... (4 entities in total)
• Functional Keywords: response regulator, dna binding protein
• Biological source: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
• Total number of polymer chains: 2
• Total formula weight: 46371.88

Authors

Chi, Y.M.,Park, A. (deposition date: 2015-05-04, release date: 2016-04-27, Last modification date: 2024-03-20)

Primary citation

Park, A.K.,Lee, J.H.,Chi, Y.M.,Park, H.
Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region
Biochem.Biophys.Res.Commun., 473:625-629, 2016

PubMed 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.

PubMed: 27038544
DOI: 10.1016/j.bbrc.2016.03.144

Experimental method

X-RAY DIFFRACTION (2.001 Å)