2h0r
Structure of the Yeast Nicotinamidase Pnc1p
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OverviewOverview
The yeast nicotinamidase Pnc1p acts in transcriptional silencing by, reducing levels of nicotinamide, an inhibitor of the histone deacetylase, Sir2p. The Pnc1p structure was determined at 2.9A resolution using MAD and, MIRAS phasing methods after inadvertent crystallization during the pursuit, of the structure of histidine-tagged yeast isocitrate dehydrogenase (IDH)., Pnc1p displays a cluster of surface histidine residues likely responsible, for its co-fractionation with IDH from Ni(2+)-coupled chromatography, resins. Researchers expressing histidine-tagged proteins in yeast should, be aware of the propensity of Pnc1p to crystallize, even when overwhelmed, in concentration by the protein of interest. The protein assembles into, extended helical arrays interwoven to form an unusually robust, yet porous, superstructure. Comparison of the Pnc1p structure with those of three, homologous bacterial proteins reveals a common core fold punctuated by, amino acid insertions unique to each protein. These insertions mediate the, self-interactions that define the distinct higher order oligomeric states, attained by these molecules. Pnc1p also acts on pyrazinamide, a substrate, analog converted by the nicotinamidase from Mycobacterium tuberculosis, into a product toxic to that organism. However, we find no evidence for, detrimental effects of the drug on yeast cell growth.
About this StructureAbout this Structure
2H0R is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Active as Nicotinamidase, with EC number 3.5.1.19 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the yeast nicotinamidase Pnc1p., Hu G, Taylor AB, McAlister-Henn L, Hart PJ, Arch Biochem Biophys. 2007 May 1;461(1):66-75. Epub 2007 Mar 2. PMID:17382284
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