1kyq

<table><tr><td colspan='2'>[[1kyq]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KYQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KYQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Met8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kyq OCA], [http://pdbe.org/1kyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kyq RCSB], [http://www.ebi.ac.uk/pdbsum/1kyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kyq ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MET8_YEAST MET8_YEAST]] Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.<ref>PMID:10051442</ref>

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== Publication Abstract from PubMed ==

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 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<ref>PMID:11980703</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1kyq" style="background-color:#fffaf0;"></div>

[[Category: Atcc 18824]]

[[Category: Brindley, A A]]

[[Category: Hill, C P]]

[[Category: Raux, E]]

[[Category: Schubert, H L]]

[[Category: Warren, M J]]

[[Category: Wilson, K S]]

[[Category: Oxidoreductase]]