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Author Wongsantichon, Jantana ♦ Yuvaniyama, Jirundon ♦ Ketterman, Albert J.
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 ♦ Genetics and evolution ♦ 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) Eukaryota ♦ Bacteria ♦ Organisms ♦ Enzymes and Coenzymes ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Genetic Phenomena ♦ Biological Sciences
Subject Keyword Discipline Crystallography ♦ Discipline Biophysics ♦ Discipline Molecular Biology ♦ Discipline Biochemistry ♦ Anopheles ♦ Enzymology ♦ Glutathione Transferase ♦ Chemistry ♦ Genetics ♦ Glutathione ♦ Amino Acid Sequence ♦ Animals ♦ Crystallization ♦ Methods ♦ Crystallography, X-ray ♦ Enzyme Stability ♦ Escherichia Coli ♦ Metabolism ♦ Point Mutation ♦ Valine ♦ Journal Article ♦ Research Support, Non-u.s. Gov't
Abstract An engineered mutant V107A of the dimeric glutathione transferase enzyme from Anopheles dirus (adgstD4-4) was cocrystallized with glutathione substrate using the hanging-drop vapour-diffusion method. The crystal diffracted to 2.47 A resolution in space group P3(2)21 (unit-cell parameters a = b = 49.4, c = 272.4 A). Although the crystal morphology differed from that previously obtained for the wild-type enzyme, the crystal packing was the same. At 318 K, the engineered mutant showed an enzyme stability that was increased by about 32-fold, while possessing a similar catalytic function to the wild type. Structural determination will provide valuable understanding of the role of Val107. This residue is in the dimeric interface and appears to contribute towards enhancing the physical properties of the entire protein.
Description Country affiliation: Thailand
Author Affiliation: Wongsantichon J ( Institute of Molecular Biology and Genetics, Mahidol University, Salaya Campus, Nakorn Pathom 73170, Thailand.)
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 2006-03-01
Publisher Place Great Britain (UK)
e-ISSN 17443091
Journal Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume Number 62
Issue Number Pt 3


Source: WHO-Global Index Medicus