PDBsum entry 4zms

DNA binding protein

PDB id

4zms

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Contents

			Protein chains

					207 a.a.

			Ligands

					BEF ×2


					4QT

			Metals

					_MG ×2

			Waters ×503

PDB id:

4zms

Links

Name:

DNA binding protein

Title:

Structure of the full-length response regulator spr1814 in complex with a phosphate analogue and b3c

Structure:

Response regulator. Chain: a, b. Engineered: yes

Source:

Streptococcus pneumoniae (strain atcc baa-255 / r6). Organism_taxid: 171101. Strain: atcc baa-255 / r6. Gene: rr11, spr1814. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.90Å

R-factor:

0.167

R-free:

0.215

Authors:

Y.M.Chi,A.Park

Key ref:

A.K.Park et al. (2016). 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. PubMed id: 27038544 DOI: 10.1016/j.bbrc.2016.03.144

Date:

04-May-15

Release date:

27-Apr-16

PROCHECK

	Headers

	References

Protein chains

Q8DNC2 (Q8DNC2_STRR6) - Response regulator from Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

Seq: Struc:					199 a.a. 207 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1016/j.bbrc.2016.03.144	Biochem Biophys Res Commun 473:625-629 (2016)
PubMed id: 27038544

Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region.
A.K.Park, J.H.Lee, Y.M.Chi, H.Park.

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.