Structure-function analysis of human protein Ero1-Lalpha.

Full Abstract

Human Ero1-Lalpha catalyzes the formation of disulfide bond and hence plays an essential role in protein folding. Understanding the mechanism of disulfide bond formation in mammals is important because of the involvement of protein misfolding in conditions such as diabetes, arthritis, cancer, and aging. However, the crystal structure of the enzyme is not available yet, which seriously hinders the understanding of biological function of Ero1-Lalpha. Based on the crystal structure of yeast Ero1p, a rational three-dimensional structural model of Ero1-Lalpha was built and the characteristics of the enzyme were hence investigated. The characteristic similarities and differences between Ero1-Lalpha and Ero1p were compared on the basis of computational and experimental results, providing the first insight into the structure-function relationships of the enzymes. Both calculation and experiment got the concordant conclusion that FAD binds more tightly with Ero1-Lalpha than Ero1p. In addition, the probable electron transfer pathway was proposed on the basis of the structural models.

Author information

Author/s: Chu, Yanyan (Y); Yang, Charles (C); Chen, Xianjun (X); Zheng, Wenyun (W); Yang, Yi (Y); Tang, Yun (Y);

Affiliation: Department of Pharmaceutical Sciences, School of Pharmacy, East China University of Science and Technology, 130 Meilong Road, Shanghai, China.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun), published in United States. (Language: eng)

Reference: 2009-Nov; vol 389 (issue 4) : pp 645-50

Dates: Created 2009/10/14; Completed 2009/11/02;

PMID: 19766098, status: MEDLINE (last retrieval date: 11/2/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

External Links for this article
(including full text providers, if available):

Click Electronic Full-text Provider Links to see options for finding the electronic full text links to this article. Note there may be a subscription or fee required for access to the full text. See our FAQ for information on finding FREE full text articles.

This article may also be located in paper journal collections available in many libraries. Use the Journal and Publication Information above to find the full article.

MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amino Acid Sequence
Electron Transport
Flavin-Adenine Dinucleotide - chemistry; metabolism
Humans
Membrane Glycoproteins - chemistry; genetics; metabolism
Models, Molecular

Models, Molecular
Molecular Sequence Data
Oxidoreductases - chemistry; genetics; metabolism
Protein Conformation
Sequence Alignment
Structure-Activity Relationship

Associated Chemicals: Membrane Glycoproteins (0) ; Flavin-Adenine Dinucleotide (146-14-5) ; ERO1L protein, human (EC 1.-) ; Oxidoreductases (EC 1.-)

These are the highest related articles currently in the database: