1kyq
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(New page: 200px<br /><applet load="1kyq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kyq, resolution 2.2Å" /> '''Met8p: A bifunctional...)
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Revision as of 17:57, 20 November 2007
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Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.
Overview
Sirohaem is a tetrapyrrole-derived prosthetic group that is required for, the essential assimilation of sulfur and nitrogen into all living systems, as part of the sulfite and nitrite reductase systems. The final two steps, in the biosynthesis of sirohaem involve a beta-NAD(+)-dependent, dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by, ferrochelation to yield sirohaem. In Saccharomyces cerevisiae, Met8p is a, bifunctional enzyme that carries out both of these reactions. Here, we, report the 2.2 A resolution crystal structure of Met8p, which adopts a, novel fold that bears no resemblance to the previously determined, structures of cobalt- or ferro-chelatases. Analysis of mutant proteins, suggests that both catalytic activities share a single active site, and, that Asp141 plays an essential role in both dehydrogenase and chelatase, processes.
About this Structure
1KYQ is a Single protein structure of sequence from Saccharomyces cerevisiae with NAD as ligand. Full crystallographic information is available from OCA.
Reference
The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase., Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ, EMBO J. 2002 May 1;21(9):2068-75. PMID:11980703
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