| Autor: |
Schubert HL; Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA. heidi@snowbird.med.utah.edu, Raux E, Warren MJ, Wilson KS |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2001 Jun; Vol. 57 (Pt 6), pp. 867-9. Date of Electronic Publication: 2001 May 25. |
| DOI: |
10.1107/s0907444901004619 |
| Abstrakt: |
Sirohaem, the prosthetic group of assimilatory sulfite and nitrite reductases, is a modified tetrapyrrole that belongs to the same fraternity of metallo-prosthetic groups as haem, chlorophyll, cobalamin and coenzyme F430 [Warren & Scott (1990), Trends Biochem Sci. 15, 486-491]. In Saccharomyces cerevisiae, the last step in the biosynthesis of sirohaem involves Met8p, a bifunctional enzyme responsible for both the NAD(+)-dependent dehydrogenation of the corrin ring and ferrochelation. Optimization of the protein storage buffer according to the results of crystallization trials resulted in a more monodisperse protein solution. Crystals were grown that diffracted to 2.1 A. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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