Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: A small angle x-ray scattering study in solution

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Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: A small angle x-ray scattering study in solution
Engineering Village 2
2006 Elsevier Inc.
Accession number: 06249935667

Title: Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: A small angle x-ray scattering study in solution

Authors: Li, Sheng-Jian; Hong, Xin-Guo; Shi, Yuan-Yuan; Li, Hui; Wang, Chih-Chen

Author affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China

Serial title: Journal of Biological Chemistry

Abbreviated serial title: J. Biol. Chem.

Volume: v 281

Issue: n 10

Issue date: Mar 10 2006

Publication year: 2006

Pages: p 6581-6588

Language: English

ISSN: 0021-9258

CODEN: JBCHA3

Document type: Journal article (JA)

Publisher: American Society for Biochemistry and Molecular Biology Inc., Bethesda, MD 20814, United States

Abstract: We presented for the first time a small angle x-ray scattering study of intact protein-disulfide isomerase (PDI) in solution. The restored model revealed that PDI is a short and roughly elliptical cylinder with a molecular mass of 69 kDa and dimensions of 105 x 65 x 40 A, and the four thioredoxin-fold domains in the order a-b-b prime -a prime are arranged in an annular fashion. Atomic force microscope imaging also supported the finding that PDI appears as an approximately flat elliptical cylinder. A PDI species with apparent molecular mass of 116 kDa measured by using size-exclusion chromatography, previously assumed to be a dimer, was determined to exist mainly as a monomer by using analytical ultracentrifugation. The C-terminal fragment 441-491 contributed to the anomalous molecular mass determination of PDI by size-exclusion chromatography. The annular model of PDI accounted for the cooperative properties of the four domains in both the isomerase and chaperone functions of PDI. ? 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Number of references: 54

Ei main heading: Enzyme kinetics

Ei controlled terms: Proteins - X ray scattering - Solutions - Atomic force microscopy - Molecular biology - Chromatography - Mathematical models

Uncontrolled terms: Protein-disulfide isomerase (PDI) - Elliptical cylinders - Molecular mass - Analytical ultracentrifugation

Ei classification codes: 461.8 Biotechnology - 804.1 Organic Compounds - 801 Chemistry - 741.3 Optical Devices & Systems - 461.9 Biology

Treatment: Literature review (LIT); Experimental (EXP)

DOI: 10.1074/jbc.M508422200

Database: Compendex

Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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