PDBsum entry: 1udd

Lipid binding protein

PDB id: 1udd

Contents

Protein chains

215 a.a. *

Waters ×155

* Residue conservation analysis

PDB id:

1udd

Name:

Lipid binding protein

Title:

Tena homologue protein from p.Horikoshii ot3

Structure:

Transcriptional regulator. Chain: a, b, c, d. Synonym: tena homologue protein ph1161. Engineered: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 70601. Strain: ot3. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dimer (from PQS)

Resolution:

2.15Å R-factor: 0.218 R-free: 0.246

Authors:

H.Itou,M.Yao,N.Watanabe,I.Tanaka

Key ref:

H.Itou et al. (2004). Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshii. Acta Crystallogr D Biol Crystallogr, 60, 1094-1100. PubMed id: 15159569 DOI: 10.1107/S0907444904008522

Date:

28-Apr-03 Release date: 01-Jun-04

Protein chains

O58873  (O58873_PYRHO) -  218aa long hypothetical transcriptional regulator

Seq: 218 a.a.

Struc: 215 a.a.

DOI no: 10.1107/S0907444904008522

Acta Crystallogr D Biol Crystallogr 60:1094-1100 (2004)

PubMed id: 15159569

Structure analysis of PH1161 protein, a transcriptional activator TenA homologue from the hyperthermophilic archaeon Pyrococcus horikoshii.

H.Itou, M.Yao, N.Watanabe, I.Tanaka.

ABSTRACT

The crystal structure of the Bacillus subtilis TenA-homologue protein PH1161 from the hyperthermophilic archaebacterium Pyrococcus horikoshii was determined. TenA is known to belong to a new family of activators that stimulate the production of extracellular proteases in B. subtilis. A sequence-similarity search revealed that TenA-homologue proteins are widespread in bacteria and archaea, suggesting that this family of proteins plays an essential role in these organisms. In the present study, the first three-dimensional structure of a member of the TenA family of proteins was determined, unexpectedly revealing that the protein has a fold identical to that of haem oxygenase-1. Analysis has also shown that the protein has a unique ligand-binding pocket. Electron density of a bound ligand molecule was observed in this pocket. These results provide a valuable insight into the functional understanding of the TenA family of proteins.

Selected figure(s)

Figure 1.
Figure 1 Ribbon representation of the PH1161 protein structure. The protein contains a dimer of dimers in the asymmetric unit, with 222 point-group symmetry. All ribbon representations were generated using MOLSCRIPT (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]) and RASTER3D (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).

Figure 2.
Figure 2 (a) Ribbon (top) and surface electric potential (bottom) representations viewed from the direction of the bottom of Fig. 1-. In surface electric potential representation, red indicates acidic and blue represents basic charged areas. Each molecule has a deep pocket between helices H5-H6 and H11-H12 and the pockets are highly charged under acidic conditions. All surface electric potential representations were generated using GRASP (Nicholls et al., 1991[Nicholls, A., Sharp, K. A. & Honig, B. (1991). Proteins Struct. Funct. Genet. 11, 281-296.]). (b) F[o] - F[c] map for the bound molecule at the acidic pocket of PH1161 protein. The map was contoured at 3 . Amino acids around the unknown bound ligand molecule are labelled: red, acidic residues; purple, hydrophobic residues; green, conserved Cys residue.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1094-1100) copyright 2004.

Figures were selected by an automated process.