PDBsum entry 4lry

Transferase/transcription regulator

PDB id: 4lry

Contents

Protein chains

356 a.a.

294 a.a.

Ligands

GOL ×2

Waters ×30

PDB id:

4lry

Name:

Transferase/transcription regulator

Title:

Crystal structure of the e.Coli dhar(n)-dhak(t79l) complex

Structure:

Pts-dependent dihydroxyacetone kinase, dihydroxyacetone- binding subunit dhak. Chain: a, b. Engineered: yes. Mutation: yes. Pts-dependent dihydroxyacetone kinase operon regulatory protein. Chain: c, d. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k-12. Gene: b1200, dhak, dhar, jw5187, ycgt. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: b1201, dhak, dhar, jw5188, ycgu.

Resolution:

2.83Å R-factor: 0.203 R-free: 0.241

Authors:

R.Shi,L.Mcdonald,M.Cygler,I.Ekiel

Key ref:

R.Shi et al. (2014). Coiled-coil helix rotation selects repressing or activating state of transcriptional regulator DhaR. Structure, 22, 478-487. PubMed id: 24440518 DOI: 10.1016/j.str.2013.11.012

Date:

21-Jul-13 Release date: 29-Jan-14

Protein chains

P76015  (DHAK_ECOLI) -  PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK from Escherichia coli (strain K12)

Seq: 356 a.a.

Struc: 356 a.a.*

Protein chains

P76016  (DHAR_ECOLI) -  PTS-dependent dihydroxyacetone kinase operon regulatory protein from Escherichia coli (strain K12)

Seq: 639 a.a.

Struc: 294 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.2.7.1.121 - phosphoenolpyruvate--glycerone phosphotransferase.
• Reaction: dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate

dihydroxyacetone (Bound ligand (Het Group name = GOL) corresponds exactly) + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2013.11.012

Structure 22:478-487 (2014)

PubMed id: 24440518

Coiled-coil helix rotation selects repressing or activating state of transcriptional regulator DhaR.

R.Shi, L.McDonald, M.Cygler, I.Ekiel.

ABSTRACT

Escherichia coli dihydroxyacetone (Dha) kinase consists of two subunits, DhaK and DhaL. Transcription of dha operon is regulated by the DhaR transcription factor and its action is under control of the kinase subunits. DhaR is activated by interaction with DhaL while it is repressed by DhaK. We have determined the structures of DhaK and DhaL bound to the tandem GAF-like and PAS domains of the DhaR, providing an architectural model for how GAF/PAS tandem domains work together in binding protein partners. The structures reveal a mechanism of opposite transcriptional regulation by the DhaK and DhaL subunits. The kinase subunits interface with DhaR through surfaces that partially overlap with their active sites, allowing sensing of ATP- versus ADP-loaded DhaL subunit and also precluding a ternary complex between DhaK-DhaL and DhaR. The rotation of helices within the DhaR coiled-coil linker upon DhaL binding provides the mechanism for transmitting the binding signal from the GAF/PAS domains to the C-terminal DNA-binding domain.