1kyq: Difference between revisions

Revision as of 11:18, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kyq.png

Template:STRUCTURE 1kyq

Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.

Template:ABSTRACT PUBMED 11980703

About this StructureAbout this Structure

1KYQ is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Wed Jul 2 11:18:47 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Met8p: A bifunctional NAD-dependent dehydrogenase and ferrochelatase involved in siroheme synthesis.'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11980703}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11980703 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11980703}}
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 [[Category: Wilson, K S.]]
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