Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.

Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Research Abstract Details 

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Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Abstract Text:

J M Lancelin,M Stein,J P Jacquot,

The recombinant form of the chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii [Jacquot et al. (1992) Nucleic Acids Res. 20, 617] that preferentially activates the NADP dependent malate dehydrogenase [EC 1.1.1.82] (m-type thioredoxin) through a light promoted reductive system, has been subjected to an extensive two-dimensional 1H NMR analysis. A complete 1H NMR assignment of the resonance lines in both the oxidized and the reduced states at pH 5.8 has been obtained allowing the recognition of the secondary structure patterns and the global protein folding. The single polypeptide chain, made of 106 residues plus one additional Met located at the N-terminal position (11.6 kDa) due to the protein expression system, folds into a pattern characteristic of the open twisted alpha/beta structures already found for Escherichia coli and human thioredoxins for which the protein shares 46 and 20% of sequence identity, respectively. The open alpha/beta structure is made of 5 beta-sheets associated in a parallel (beta 1 to beta 3) and anti parallel manner (beta 3 to beta 5) and surrounded by 4 helices. This represents the first structural exploratory study of the ubiquitous oxido-reductase thioredoxins in a photosynthetic living system.

Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Publishing Authors By Initials

JM Lancelin,M Stein,JP Jacquot,

For similar proteins: thioredoxins research abstracts see: proteins: thioredoxins research

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Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 114

Page Numbers: 421-31

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1993

Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Keywords Mesh Terms:

KEYWORDS: Thioredoxins

MESH TERMS: chemistry

Chemical & Substance for Abstract: Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Information

Substance Name: Thioredoxins

Registry Number: 52500-60-4

Grant and Affiliation Information for Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR.

AFFILIATION: Institut de Biologie Structurale CEA-CNRS, Grenoble, France.

Country: JAPAN

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MEDLINETA: J Biochem

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