PDBsum entry 1gh2

Electron transport

PDB id: 1gh2

Contents

Protein chain

107 a.a. *

Waters ×44

* Residue conservation analysis

PDB id:

1gh2

Name:

Electron transport

Title:

Crystal structure of the catalytic domain of a new human thioredoxin- like protein

Structure:

Thioredoxin-like protein. Chain: a. Fragment: residues 2 - 108, catalytic n-terminal domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Tissue: fetal brain. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.22Å R-factor: 0.221 R-free: 0.253

Authors:

J.Jin,X.Chen,Q.Guo,J.Yuan,B.Qiang,Z.Rao

Key ref:

J.Jin et al. (2002). Crystal structure of the catalytic domain of a human thioredoxin-like protein. Eur J Biochem, 269, 2060-2068. PubMed id: 11985582 DOI: 10.1046/j.1432-1033.2002.02844.x

Date:

01-Nov-00 Release date: 01-May-01

Protein chain

O43396  (TXNL1_HUMAN) -  Thioredoxin-like protein 1 from Homo sapiens

Seq: 289 a.a.

Struc: 107 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1046/j.1432-1033.2002.02844.x

Eur J Biochem 269:2060-2068 (2002)

PubMed id: 11985582

Crystal structure of the catalytic domain of a human thioredoxin-like protein.

J.Jin, X.Chen, Y.Zhou, M.Bartlam, Q.Guo, Y.Liu, Y.Sun, Y.Gao, S.Ye, G.Li, Z.Rao, B.Qiang, J.Yuan.

ABSTRACT

Thioredoxin is a ubiquitous dithiol oxidoreductase found in many organisms and involved in numerous biochemical processes. Human thioredoxin-like protein (hTRXL) is differentially expressed at different development stages of human fetal cerebrum and belongs to an expanding family of thioredoxins. We have solved the crystal structure of the recombinant N-terminal catalytic domain (hTRXL-N) of hTRXL in its oxidized form at 2.2-A resolution. Although this domain shares a similar three-dimensional structure with human thioredoxin (hTRX), a unique feature of hTRXL-N is the large number of positively charged residues distributed around the active site, which has been implicated in substrate specificity. Furthermore, the hTRXL-N crystal structure is monomeric while hTRX is dimeric in its four crystal structures (reduced, oxidized, C73S and C32S/C35S mutants) reported to date. As dimerization is the key regulatory factor in hTRX, the positive charge and lack of dimer formation of hTRXL-N suggest that it could interact with the acidic amino-acid rich C-terminal region, thereby suggesting a novel regulation mechanism.

Selected figure(s)

Figure 1.
Fig. 1. Expression pattern of the hTRXL transcript. Differential expression of hTRXL in human fetal cerebrum of 33- and 13-weeks-old. Human adult tissue Poly(A^+) RNA Northern blot (ClonTech). The ^32P-labeled probe is the EST obtained from DDRT-PCR (GenBank accession no. U48630) and the control used is -actin cDNA (ClonTech).

Figure 7.
Fig. 7. Molecular surface comparison between hTRX and hTRXL-N. Molecular surface representations of hTRX (A) and hTRXL-N (B) around the active surface in the same orientation were produced using GRASP. Electrostatic surface potentials are contoured from -30 (red) to 30 (blue) k[b]T·e^-1. The ellipses highlight the position of active site in hTRX and hTRXL-N, respectively.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2002, 269, 2060-2068) copyright 2002.

Figures were selected by an automated process.