PDBsum entry 2a0b

Sensory transduction

PDB id: 2a0b

Contents

Protein chain

118 a.a. *

Metals

_ZN

Waters ×156

* Residue conservation analysis

PDB id:

2a0b

Name:

Sensory transduction

Title:

Histidine-containing phosphotransfer domain of arcb from escherichia coli

Structure:

Hpt domain. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: dz225.

Resolution:

1.57Å R-factor: 0.190 R-free: 0.245

Authors:

M.Kato,T.Mizuno,T.Shimizu,T.Hakoshima

Key ref:

M.Kato et al. (1999). Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution. Acta Crystallogr D Biol Crystallogr, 55, 1842-1849. PubMed id: 10531481 DOI: 10.1107/S0907444999010392

Date:

02-Apr-98 Release date: 17-Jun-98

Protein chain

P0AEC3  (ARCB_ECOLI) -  Aerobic respiration control sensor protein ArcB from Escherichia coli (strain K12)

Seq: 778 a.a.

Struc: 118 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

reference

DOI no: 10.1107/S0907444999010392

Acta Crystallogr D Biol Crystallogr 55:1842-1849 (1999)

PubMed id: 10531481

Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution.

M.Kato, T.Mizuno, T.Shimizu, T.Hakoshima.

ABSTRACT

The crystal structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli has been refined to 1.57 A resolution, using the coordinates of the earlier 2.06 A structure as a starting model. The final model contained 956 protein atoms, one zinc ion and 156 water molecules, with an R factor of 19.0%. The high-resolution electron-density maps clearly revealed additional solvent molecules and seven discrete rotamers in the protein side chains. One residue, Met755, was fully buried but was able to occupy the space in the hydrophobic core by means of the two-state conformation of its side chain. One water molecule was buried in the protein core and contributed to the rigidity of the HPt domain, cooperating in the coordination of the zinc ion.

Selected figure(s)

Figure 2.
Figure 2 Discrete rotamers with their electron densities. The residues are shown as ball-and-stick models. The densities are contoured at the 1.0 level.

Figure 4.
Figure 4 Stereo diagram of the Zn2+-binding site and buried water molecule. All residues are shown as ball-and-stick models, with water molecules (W6 and W7) and the Zn2+ ion as spheres. Dashed lines indicate hydrogen bonds or coordinations to Zn2+.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1842-1849) copyright 1999.

Figures were selected by an automated process.