PDBsum entry 4cb0

Transferase

PDB id: 4cb0

Contents

Protein chains

240 a.a.

220 a.a.

Ligands

ATP ×2

SO4 ×5

PDB id:

4cb0

Name:

Transferase

Title:

Crystal structure of cpxahdc in complex with atp (hexagonal form)

Structure:

Sensor protein cpxa. Chain: a, b. Fragment: cytoplasmic region, residues 188-457. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 83333. Strain: k-12. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

3.30Å R-factor: 0.204 R-free: 0.229

Authors:

A.E.Mechaly,N.Sassoon,J.M.Betton,P.M.Alzari

Key ref:

A.E.Mechaly et al. (2014). Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation. Plos Biol, 12, e1001776. PubMed id: 24492262 DOI: 10.1371/journal.pbio.1001776

Date:

09-Oct-13 Release date: 12-Feb-14

Protein chain

P0AE82  (CPXA_ECOLI) -  Sensor histidine kinase CpxA from Escherichia coli (strain K12)

Seq: 457 a.a.

Struc: 240 a.a.

Protein chain

P0AE82  (CPXA_ECOLI) -  Sensor histidine kinase CpxA from Escherichia coli (strain K12)

Seq: 457 a.a.

Struc: 220 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.2.7.13.3 - histidine kinase.
• Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

ATP (Bound ligand (Het Group name = ATP) corresponds exactly) + protein L-histidine = ADP + protein N-phospho-L-histidine

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

reference

DOI no: 10.1371/journal.pbio.1001776

Plos Biol 12:e1001776 (2014)

PubMed id: 24492262

Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.

A.E.Mechaly, N.Sassoon, J.M.Betton, P.M.Alzari.

ABSTRACT

Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK α-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.