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Author Stefankova, Petra ♦ Maderova, Jana ♦ Barak, Imrich ♦ Kollarova, Marta ♦ Otwinowski, Zbyszek
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher Wiley
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Crystallography ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Natural history of organisms ♦ Microorganisms, fungi & algae ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Bacteria ♦ Organisms ♦ Amino Acids, Peptides, and Proteins ♦ Nucleic Acids, Nucleotides, and Nucleosides ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Equipment and Supplies ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Biological Sciences
Subject Keyword Discipline Crystallography ♦ Discipline Biophysics ♦ Discipline Molecular Biology ♦ Discipline Biochemistry ♦ Streptomyces Coelicolor ♦ Chemistry ♦ Thioredoxins ♦ Amino Acid Sequence ♦ Bacterial Proteins ♦ Base Sequence ♦ Binding Sites ♦ Cloning, Molecular ♦ Conserved Sequence ♦ Crystallography, X-ray ♦ Dna Primers ♦ Escherichia Coli ♦ Models, Molecular ♦ Protein Structure, Secondary ♦ Sequence Alignment ♦ Synchrotrons ♦ Journal Article ♦ Research Support, Non-u.s. Gov't ♦ Research Support, U.s. Gov't, Non-p.h.s.
Abstract Thioredoxins are ubiquitous proteins that serve as reducing agents and general protein disulfide reductases. In turn, they are reduced by electrons obtained from the NADPH-containing thioredoxin reductase. Thioredoxins have been isolated and characterized from a large number of organisms. The Gram-positive bacterium Streptomyces coelicolor contains three thioredoxins that are involved in unknown biological processes. trxA from S. coelicolor was cloned and expressed in Escherichia coli and the protein purified and crystallized using the hanging-drop method of vapour diffusion. The crystal structure of thioredoxin A has been determined at 1.5 A resolution using a synchrotron-radiation source. The protein reveals a thioredoxin-like fold with a typical CXXC active site. The crystal exhibits the symmetry of space group P2(1)2(1)2, with unit-cell parameters a = 43.6, b = 71.8, c = 33.2 A.
Description Author Affiliation: Stefankova P ( Department of Biochemistry, Faculty of Natural Sciences, Comenius University, Mlynska dolina CH-1, 842 15 Bratislava, Slovak Republic.)
ISSN 2053230X
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2005-02-01
Publisher Place Great Britain (UK)
e-ISSN 17443091
Journal Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume Number 61
Issue Number Pt 2


Source: WHO-Global Index Medicus