PDBsum entry 1v98

Oxidoreductase

PDB id: 1v98

Contents

Protein chains

92 a.a. *

Ligands

SO4 ×3

Metals

_MG ×2

Waters ×197

* Residue conservation analysis

PDB id:

1v98

Name:

Oxidoreductase

Title:

Crystal structure analysis of thioredoxin from thermus thermophilus

Structure:

Thioredoxin. Chain: a, b. Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.82Å R-factor: 0.195 R-free: 0.236

Authors:

P.H.Rehse,T.H.Tahirov,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

P.H.Rehse et al. (2005). Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus. Proteins, 61, 1032-1037. PubMed id: 16245350 DOI: 10.1002/prot.20623

Date:

21-Jan-04 Release date: 01-Feb-05

Protein chains

Q5SI93  (Q5SI93_THET8) -  Thioredoxin from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 140 a.a.

Struc: 92 a.a.

Enzyme reactions

• Enzyme class: E.C.1.8.1.9 - thioredoxin-disulfide reductase (NADPH).
• Reaction: [thioredoxin]-dithiol + NADP⁺ = [thioredoxin]-disulfide + NADPH + H⁺

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

Added reference

DOI no: 10.1002/prot.20623

Proteins 61:1032-1037 (2005)

PubMed id: 16245350

Compact reduced thioredoxin structure from the thermophilic bacteria Thermus thermophilus.

P.H.Rehse, M.Kumei, T.H.Tahirov.

ABSTRACT

The X-ray crystallographic structure of a thioredoxin from Thermus thermophilus was solved to 1.8 A resolution by molecular replacement. The crystals' space group was C2 with cell dimensions of a = 40.91, b = 95.44, c = 56.68 A, beta =91.41 degrees, with two molecules in the asymmetric unit. Unlike the reported thioredoxin structures, the biological unit of T. thermophilus thioredoxin is a dimer both in solution and in the crystal. The fold conforms to the "thioredoxin fold" that is common over a class of nine protein families including thioredoxin; however, the folded portion of this protein is much more compact than other thioredoxins previously solved by X-ray crystallography being reduced by one alpha-helix and one beta-strand. As with other thioredoxins, the active site is highly conserved even though the variation in sequence can be quite large. The T. thermophilus thioredoxin has some variability at the active site, especially compared with previously solved structures from bacterial sources.

Selected figure(s)

Figure 2.
Figure 2. Dimer generated by monomers in the asymmetric unit orientated to show loop penetration. Labeling convention is the thioredoxin standard and therefore starts at 2 and 2. The prime refers to the second monomer.

Figure 4.
Figure 4. Active site of the T. thermophilus thioredoxin. Residues in blue refer to the human structure, in red to A. acidcaldarius. Residue labels correspond to the T. thermophilus structure unless there is an h tag which refers to human.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 61, 1032-1037) copyright 2005.

Figures were selected by an automated process.