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Crystallization of Biological Macromolecules
- Publisher
- Wiley
- Copyright
- Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309107010731
- pmid
- 17401193
- Publisher site
- See Article on Publisher Site
Abstract
Physarum polycephalum cytochrome b5 reductase catalyzes the reduction of cytochrome b5 by NADH. The structure of P. polycephalum cytochrome b5 reductase was determined at a resolution of 1.56 Å. The molecular structure was compared with that of human cytochrome b5 reductase, which had previously been determined at 1.75 Å 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.
Journal
Acta Crystallographica Section F – Wiley
Published: Apr 1, 2007