TAILIEUCHUNG - Báo cáo khoa học: Crystal structure of RNase A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor

Rv3619c and Rv3620c are the secretory, antigenic proteins of the ESAT-6⁄CFP-10 family ofMycobacterium tuberculosisH37Rv. In this article, we show that Rv3619c interacts with Rv3620c to form a 1 : 1 heterodimeric complex with a dissociation constant (Kd) of ·10 )7 M. The thermal unfolding of the heterodimer was completely reversible, with a Tm of 48 C. | IFEBS Journal Crystal structure of RNase A tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor Ulrich Arnold Franziska Leich Piotr Neumannf Hauke Lilie and Renate Ulbrich-Hofmann Department of Biochemistry and Biotechnology Martin-Luther University Halle-Wittenberg Halle Germany Keywords crystal structure proteolysis ribonuclease inhibitor stoichiometry RNase A tandem enzyme Correspondence U. Arnold Department of Biochemistry and Biotechnology Martin-Luther University Halle-Wittenberg Kurt-Mothes Str. 3 06120 Halle Germany Fax 49 345 5527303 Tel 49 345 5524865 E-mail . Website http . biotech Present addresses Institute of MedicalImmunology Martin-Luther-University Halle-Wittenberg Magde-burger Str. 2 06097 Halle Germany Institute of Microbiology and Genetics Georg-August University Gottingen Justus-von-Liebig-Weg 11 37077 Gottingen Germany Database Structuraldata are available in the Protein Data Bank under the accession numbers 3MX8 3MWR and 3MWQ Received 27 August 2010 revised 3 November 2010 accepted 8 November 2010 doi Because of their ability to degrade RNA RNases are potent cytotoxins. The cytotoxic activity of most members of the RNase A superfamily however is abolished by the cytosolic ribonuclease inhibitor RI . RNase A tandem enzymes in which two RNase A molecules are artificially connected by a peptide linker and thus have a pseudodimeric structure exhibit remarkable cytotoxic activity. In vitro however these enzymes are still inhibited by RI. Here we present the crystal structures of three tandem enzymes with the linker sequences GPPG SGSGSG and SGRSGRSG which allowed us to analyze the mode of binding of RI to the RNase A tandem enzymes. Modeling studies with the crystal structures of the RI-RNase A complex and the SGRSGRSG-RNase A tandem enzyme as templates suggested a 1 1 binding stoichiometry for the RI-RNase A tandem enzyme .

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