PDBsum entry: 1joy

Transferase

PDB id: 1joy

Contents

Protein chains

67 a.a. *

* Residue conservation analysis

PDB id:

1joy

Name:

Transferase

Title:

Solution structure of the homodimeric domain of envz from escherichia coli by multi-dimensional nmr.

Structure:

Protein (envz_ecoli). Chain: a, b. Fragment: residues 223-289. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

21 models

Authors:

C.Tomomori,T.Tanaka,R.Dutta,H.Park,S.K.Saha,Y.Zhu,R.Ishima, D.Liu,K.I.Tong,H.Kurokawa,H.Qian,M.Inouye,M.Ikura

Key ref:

C.Tomomori et al. (1999). Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ. Nat Struct Biol, 6, 729-734. PubMed id: 10426948 DOI: 10.1038/11495

Date:

28-Dec-98 Release date: 12-Jan-00

Protein chains

P0AEJ4  (ENVZ_ECOLI) -  Osmolarity sensor protein EnvZ

Seq: 450 a.a.

Struc: 67 a.a.

Enzyme reactions

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

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

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (1 term)
• Biological process: signal transduction (1 term)
• Biochemical function: signal transducer activity (2 terms)

reference

DOI no: 10.1038/11495

Nat Struct Biol 6:729-734 (1999)

PubMed id: 10426948

Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ.

C.Tomomori, T.Tanaka, R.Dutta, H.Park, S.K.Saha, Y.Zhu, R.Ishima, D.Liu, K.I.Tong, H.Kurokawa, H.Qian, M.Inouye, M.Ikura.

ABSTRACT

Escherichia coli osmosensor EnvZ is a protein histidine kinase that plays a central role in osmoregulation, a cellular adaptation process involving the His-Asp phosphorelay signal transduction system. Dimerization of the transmembrane protein is essential for its autophosphorylation and phosphorelay signal transduction functions. Here we present the NMR-derived structure of the homodimeric core domain (residues 223-289) of EnvZ that includes His 243, the site of autophosphorylation and phosphate transfer reactions. The structure comprises a four-helix bundle formed by two identical helix-turn-helix subunits, revealing the molecular assembly of two active sites within the dimeric kinase.

Selected figure(s)

Figure 3.
Figure 3. Interaction between EnvZ and OmpR. a, Two views of the molecular surface are colored according to electrostatic potential. Negative potential is colored in red and positive potential in blue. To highlight the inter-subunit surface, residue numbers of one subunit are shown in blue and those of the other subunit in black. In the vicinity of His 243 and Thr 247, an acidic patch is formed by Asp 244 from one subunit and by Asp 273 and Glu 276 from the other subunit (left hand panel). An additional acidic cluster, involving Asp 232 and Asp 233 from one subunit and Asp 286 from the other subunit, is at the same molecular face as the other acidic cluster, but is distant from His 243. Arg 246 is also close to His 243 (right hand panel). The image in the left panel is related to that in the right panel by a 90° rotation along the vertical axis. b, OmpR-induced changes in intensity of the backbone peaks in ^1H-^15N HSQC spectra of EnvZ domain A. A series of ^1H-^15N HSQC spectra were recorded at each of the following ratios: [OmpR(1−134)]/[EnvZ] = 0.0, 0.2, 0.4, 0.6, 0.8, and 1.0. Only the spectra at ratios 0.0 (left) and 0.2 (right) are shown. Peak intensities were analyzed with nmrDraw and PIPP software. Peaks that displayed very large changes are boxed. c, The changes in cross peak intensities in the HSQC spectra in the titration experiment are classified into four groups (very large, large, medium, and small) and shown in red, orange, yellow, and green, respectively, on the ribbon diagram of EnvZ domain A. The conserved His 243 as well as the N- and C- termini are marked.

Figure 4.
Figure 4. Summary of mutations in EnvZ domain A. Mutations in domain A that affect EnvZ functions^14, ^15 are summarized in the space filling model. Mutations that resulted in kinase-/phosphatase+ are colored in green, and kinase+/phosphatase- in light blue. The two subunits are colored in pink and yellow as in Fig. 1. The inter-subunit interface is shown in the left hand panel and the intra-subunit interface in the right hand panel.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (1999, 6, 729-734) copyright 1999.

Figures were selected by an automated process.