NDLI: Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.

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Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.

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Structure of Physarum polycephalum cytochrome b5 reductase at 1.56 A resolution.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kim, Sangwoo Suga, Michihiro Ogasahara, Kyoko Ikegami, Terumi Minami, Yoshiko Yubisui, Toshitsugu Tsukihara, Tomitake
Description	Country affiliation: Japan Author Affiliation: Kim S ( Institute for Protein Research, Osaka University, 3-2 Yamada-oka, Suita, Osaka, Japan.)
Abstract	Physarum polycephalum cytochrome b(5) reductase catalyzes the reduction of cytochrome b(5) by NADH. The structure of P. polycephalum cytochrome b(5) reductase was determined at a resolution of 1.56 A. The molecular structure was compared with that of human cytochrome b(5) reductase, which had previously been determined at 1.75 A resolution [Bando et al. (2004), Acta Cryst. D60, 1929-1934]. The high-resolution structure revealed conformational differences between the two enzymes in the adenosine moiety of the FAD, the lid region and the linker region. The structural properties of both proteins were inspected in terms of hydrogen bonding, ion pairs, accessible surface area and cavity volume. The differences in these structural properties between the two proteins were consistent with estimates of their thermostabilities obtained from differential scanning calorimetry data.
File Format	HTM / HTML
ISSN	2053230X
e-ISSN	17443091
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Issue Number	Pt 4
Volume Number	63
Language	English
Publisher	Wiley
Publisher Date	2007-04-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Crystallography Discipline Biophysics Discipline Molecular Biology Discipline Biochemistry Cytochromes B5 Chemistry Physarum Polycephalum Enzymology Animals Calorimetry, Differential Scanning Crystallography, X-ray Metabolism Flavin-adenine Dinucleotide Hydrogen Bonding Protein Conformation
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Medicine Biochemistry Biophysics Condensed Matter Physics

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