PDBsum entry 6jgx

Transcription/DNA

PDB id: 6jgx

Contents

Protein chains

143 a.a.

136 a.a.

DNA/RNA

Metals

_CD ×4

PDB id:

6jgx

Name:

Transcription/DNA

Title:

Crystal structure of the transcriptional regulator cadr from p. Putida in complex with cadmium(ii) and DNA

Structure:

Cadr. Chain: a, b. Synonym: cd(ii)/pb(ii)-responsive transcriptional regulator. Engineered: yes. DNA (5'- d( Cp Ap Cp Cp Cp Tp Ap Tp Ap Gp Tp Gp Gp Cp Tp Ap Cp Ap Gp Gp Gp T)- 3'). Chain: c. Engineered: yes.

Source:

Pseudomonas putida. Arthrobacter siderocapsulatus. Organism_taxid: 303. Atcc: 47054. Gene: cadr, biw19_10095, bl240_26950. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 303

Resolution:

2.71Å R-factor: 0.211 R-free: 0.233

Authors:

X.C.Liu,J.H.Gan,H.Chen

Key ref:

X.Liu et al. (2019). Selective cadmium regulation mediated by a cooperative binding mechanism in CadR. Proc Natl Acad Sci U S A, 116, 20398-20403. PubMed id: 31548408 DOI: 10.1073/pnas.1908610116

Date:

15-Feb-19 Release date: 25-Sep-19

Protein chain

Q93TP7  (Q93TP7_PSEPU) -  CadR from Pseudomonas putida

Seq: 147 a.a.

Struc: 143 a.a.

Protein chain

Q93TP7  (Q93TP7_PSEPU) -  CadR from Pseudomonas putida

Seq: 147 a.a.

Struc: 136 a.a.

DNA/RNA chains

C-A-C-C-C-T-A-T-A-G-T-G-G-C-T-A-C-A-G-G-G-T 22 bases

G-A-C-C-C-T-G-T-A-G-C-C-A-C-T-A-T-A-G-G-G-T 22 bases

DOI no: 10.1073/pnas.1908610116

Proc Natl Acad Sci U S A 116:20398-20403 (2019)

PubMed id: 31548408

Selective cadmium regulation mediated by a cooperative binding mechanism in CadR.

X.Liu, Q.Hu, J.Yang, S.Huang, T.Wei, W.Chen, Y.He, D.Wang, Z.Liu, K.Wang, J.Gan, H.Chen.

ABSTRACT

Detoxification of the highly toxic cadmium element is essential for the survival of living organisms. Pseudomonas putida CadR, a MerR family transcriptional regulator, has been reported to exhibit an ultraspecific response to the cadmium ion. Our crystallographic and spectroscopic studies reveal that the extra cadmium selectivity of CadR is mediated by the unexpected cooperation of thiolate-rich site I and histidine-rich site II. Cadmium binding in site I mediates the reorientation of protein domains and facilitates the assembly of site II. Subsequently, site II bridge-links 2 DNA binding domains through ligands His140/His145 in the C-terminal histidine-rich tail. With dynamic transit between 2 conformational states, this bridge could stabilize the regulator into an optimal conformation that is critical for enhancing the transcriptional activity of the cadmium detoxification system. Our results provide dynamic insight into how nature utilizes the unique cooperative binding mechanism in multisite proteins to recognize cadmium ions specifically.