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(2): 625-9, 2016 Apr 29.
Article
em En
| MEDLINE
| ID: mdl-27038544
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-ß5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.
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Base de dados:
MEDLINE
Assunto principal:
Fosfatos
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Streptococcus pneumoniae
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Proteínas de Bactérias
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Proteínas de Ligação a DNA
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article