PDBsum entry 2mlk

Signaling protein

PDB id: 2mlk

Contents

Protein chain

110 a.a.

PDB id:

2mlk

Name:

Signaling protein

Title:

Three-dimensional structure of thE C-terminal DNA-binding domain of rsta protein from klebsiella pneumoniae

Structure:

Rsta. Chain: a. Fragment: DNA-binding domain (unp residues 131-239). Synonym: transcriptional regulator. Engineered: yes

Source:

Klebsiella pneumoniae. Organism_taxid: 573. Gene: d364_07465. Expressed in: escherichia coli. Expression_system_taxid: 511693.

NMR struc:

20 models

Authors:

P.Fang,S.Chen,Y.Cheng,C.Chang,T.Yu,T.Huang

Key ref:

Y.C.Li et al. (2014). Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element. Nucleic Acids Res, 42, 8777-8788. PubMed id: 24990372 DOI: 10.1093/nar/gku572

Date:

02-Mar-14 Release date: 16-Jul-14

Protein chain

U5MDD9  (U5MDD9_KLEPN) -

DOI no: 10.1093/nar/gku572

Nucleic Acids Res 42:8777-8788 (2014)

PubMed id: 24990372

Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element.

Y.C.Li, C.K.Chang, C.F.Chang, Y.H.Cheng, P.J.Fang, T.Yu, S.C.Chen, Y.C.Li, C.D.Hsiao, T.H.Huang.

ABSTRACT

The RstA/RstB system is a bacterial two-component regulatory system consisting of the membrane sensor, RstB and its cognate response regulator (RR) RstA. The RstA of Klebsiella pneumoniae (kpRstA) consists of an N-terminal receiver domain (RD, residues 1-119) and a C-terminal DNA-binding domain (DBD, residues 130-236). Phosphorylation of kpRstA induces dimerization, which allows two kpRstA DBDs to bind to a tandem repeat, called the RstA box, and regulate the expression of downstream genes. Here we report the solution and crystal structures of the free kpRstA RD, DBD and DBD/RstA box DNA complex. The structure of the kpRstA DBD/RstA box complex suggests that the two protomers interact with the RstA box in an asymmetric fashion. Equilibrium binding studies further reveal that the two protomers within the kpRstA dimer bind to the RstA box in a sequential manner. Taken together, our results suggest a binding model where dimerization of the kpRstA RDs provides the platform to allow the first kpRstA DBD protomer to anchor protein-DNA interaction, whereas the second protomer plays a key role in ensuring correct recognition of the RstA box.