PDBsum entry 1id0

Transferase

PDB id: 1id0

Contents

Protein chain

146 a.a. *

Ligands

ANP

Metals

_MG

Waters ×189

* Residue conservation analysis

PDB id:

1id0

Name:

Transferase

Title:

Crystal structure of the nucleotide bond conformation of phoq kinase domain

Structure:

Phoq histidine kinase. Chain: a. Fragment: kinase domain. Synonym: sensor protein phoq. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.60Å R-factor: 0.199 R-free: 0.233

Authors:

A.Marina,C.Mott,A.Auyzenberg,C.D.Waldburger,W.A.Hendrickson

Key ref:

A.Marina et al. (2001). Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism. J Biol Chem, 276, 41182-41190. PubMed id: 11493605 DOI: 10.1074/jbc.M106080200

Date:

02-Apr-01 Release date: 17-Oct-01

Protein chain

P23837  (PHOQ_ECOLI) -  Sensor protein PhoQ from Escherichia coli (strain K12)

Seq: 486 a.a.

Struc: 146 a.a.

Enzyme reactions

• Enzyme class 1: 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 81.25% similarity) + protein N-phospho-L-histidine

• Enzyme class 2: E.C.3.1.3.- - ?????

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

DOI no: 10.1074/jbc.M106080200

J Biol Chem 276:41182-41190 (2001)

PubMed id: 11493605

Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanism.

A.Marina, C.Mott, A.Auyzenberg, W.A.Hendrickson, C.D.Waldburger.

ABSTRACT

PhoQ is a transmembrane histidine kinase belonging to the family of two-component signal transducing systems common in prokaryotes and lower eukaryotes. In response to changes in environmental Mg(2+) concentration, PhoQ regulates the level of phosphorylated PhoP, its cognate transcriptional response-regulator. The PhoQ cytoplasmic region comprises two independently folding domains: the histidine-containing phosphotransfer domain and the ATP-binding kinase domain. We have determined the structure of the kinase domain of Escherichia coli PhoQ complexed with the non-hydrolyzable ATP analog adenosine 5'-(beta,gamma-imino)triphosphate and Mg(2+). Nucleotide binding appears to be accompanied by conformational changes in the loop that surrounds the ATP analog (ATP-lid) and has implications for interactions with the substrate phosphotransfer domain. The high resolution (1.6 A) structure reveals a detailed view of the nucleotide-binding site, allowing us to identify potential catalytic residues. Mutagenic analyses of these residues provide new insights into the catalytic mechanism of histidine phosphorylation in the histidine kinase family. Comparison with the active site of the related GHL ATPase family reveals differences that are proposed to account for the distinct functions of these proteins.

Selected figure(s)

Figure 3.
Fig. 3. ATP-lid movement in PhoQ-KD nucleotide-bound structure. Superimposition of C traces from PhoQ-KD (blue) and CheA-KD (yellow) shows the ATP-lid displacement toward the main -sheet in PhoQ (closed conformation). The AMPPNP molecule is shown in magenta. Glycine C atoms are shown as spheres, and side chains of the hydrophobic patch residues are shown as sticks. Selected residues are labeled for each protein in the color corresponding to the backbone trace. hairpin movement and the conserved Gly in the hairpin are also indicated.

Figure 4.
Fig. 4. AMPPNP binding site. Upper panel, plot of the interactions between AMPPNP-Mg2+ and the protein drawn with the program LIGPLOT (40). Lower panel, stereoview of structural elements that form the ATP binding site in PhoQ-KD. Helices and strands are partially transparent with the same colors as in Fig. 1A. the AMPPNP molecule (yellow) and interacting side chains (green) are depicted as ball-and-stick with the same colors as in upper panel. Carbon, nitrogen, oxygen, and phosphate are drawn in gray, blue, red, and black, respectively. Water molecules are cyan spheres, and the Mg2+ ion is a green sphere. Hydrogen bonds are shown as dotted magenta lines and the magnesium coordination as dotted black lines.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 41182-41190) copyright 2001.

Figures were selected by an automated process.