PDBsum entry: 1bxd

Transferase

PDB id: 1bxd

Contents

Protein chain

161 a.a. *

Ligands

ANP

* Residue conservation analysis

PDB id:

1bxd

Name:

Transferase

Title:

Nmr structure of the histidine kinase domain of the e. Coli osmosensor envz

Structure:

Protein (osmolarity sensor protein (envz)). Chain: a. Fragment: residues 290-450. Synonym: envz(290-450). Engineered: yes

Source:

Escherichia coli bl21(de3). Organism_taxid: 469008. Strain: bl21-de3. Cellular_location: cytoplasm. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

T.Tanaka,S.K.Saha,C.Tomomori,R.Ishima,D.Liu,K.I.Tong,H.Park, R.Dutta,L.Qin,M.B.Swindells,T.Yamazaki,A.M.Ono,M.Kainosho, M.Inouye,M.Ikura

Key ref:

T.Tanaka et al. (1998). NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ. Nature, 396, 88-92. PubMed id: 9817206 DOI: 10.1038/23968

Date:

02-Oct-98 Release date: 02-Oct-99

Protein chain

P0AEJ4  (ENVZ_ECOLI) -  Osmolarity sensor protein EnvZ

Seq: 450 a.a.

Struc: 161 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

ATP + protein L-histidine = ADP (Bound ligand (Het Group name = ANP) matches with 81.00% similarity) + protein N-phospho-L-histidine

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

 Gene Ontology (GO) functional annotation 

• Biological process: signal transduction (3 terms)
• Biochemical function: transferase activity, transferring phosphorus-containing groups (4 terms)

reference

DOI no: 10.1038/23968

Nature 396:88-92 (1998)

PubMed id: 9817206

NMR structure of the histidine kinase domain of the E. coli osmosensor EnvZ.

T.Tanaka, S.K.Saha, C.Tomomori, R.Ishima, D.Liu, K.I.Tong, H.Park, R.Dutta, L.Qin, M.B.Swindells, T.Yamazaki, A.M.Ono, M.Kainosho, M.Inouye, M.Ikura.

ABSTRACT

Bacteria live in capricious environments, in which they must continuously sense external conditions in order to adjust their shape, motility and physiology. The histidine-aspartate phosphorelay signal-transduction system (also known as the two-component system) is important in cellular adaptation to environmental changes in both prokaryotes and lower eukaryotes. In this system, protein histidine kinases function as sensors and signal transducers. The Escherichia coli osmosensor, EnvZ, is a transmembrane protein with histidine kinase activity in its cytoplasmic region. The cytoplasmic region contains two functional domains: domain A (residues 223-289) contains the conserved histidine residue (H243), a site of autophosphorylation as well as transphosphorylation to the conserved D55 residue of response regulator OmpR, whereas domain B (residues 290-450) encloses several highly conserved regions (G1, G2, F and N boxes) and is able to phosphorylate H243. Here we present the solution structure of domain B, the catalytic core of EnvZ. This core has a novel protein kinase structure, distinct from the serine/threonine/tyrosine kinase fold, with unanticipated similarities to both heatshock protein 90 and DNA gyrase B.

Selected figure(s)

Figure 3.
Figure 3 EnvZ and Hsp90 have a similar fold in their ATP-binding regions. a, Ribbon representation of the EnvZ catalytic domain and the ATP-binding domain of the molecular chaperone Hsp90 (Protein DataBank accession number 1amw)9. For the EnvZ catalytic domain, strand B is shown in yellow, strand D in orange, strand E in light blue, strands F and G in purple, helix 2 in pink, and the central loop including helices 3 and 4 in green. Heavy atoms (except N, C and O) of N347 (in blue), D373, G375, G377 and I378 (in yellow), and G403, L404, G405 and L406 (in magenta) are shown as ball-and-stick models. The corresponding secondary structural elements and specific residues of Hsp90 are coloured as for EnvZ. AMP-PNP (ADP in Hsp90) is also shown as a ball-and-stick model, in red. The model was generated using MOLSCRIPT20 and Raster3D^21. b, Alignment of the amino-acid sequences of the EnvZ catalytic domain and the ATP-binding domains of Hsp90 and DNA gyrase B (GyrB)9,22, found by the SSAP program23. -Helices and -strands of each structure are indicated as cylinders and arrows, respectively. The colour coding for the secondary structure elements and highlighted residues is as in a.

Figure 4.
Figure 4 The EnvZ catalytic domain and DNA gyrase B. a, Secondary structure; b, the linear arrangement of structural elements. This figure emphasizes the recurrence of aligned structural elements involved in the ATP-binding sites (coloured) and the position of the left-handed motif in each structure (EnvZ, yellow-pink-orange; DNA gyrase B, hashed regions of the same colours). -Helices and -strands of each structure are indicated as cylinders and arrows, respectively. The colour coding for the secondary structure elements is the same as in Fig. 3a except for the C-terminal domain of the DNA gyrase B subunit. The N and C termini of each structure are indicated.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (1998, 396, 88-92) copyright 1998.

Figures were selected by an automated process.