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Crystal structure of the N‐terminal domain of human SIRT7 reveals a three‐helical domain architecture.

Proteins.. 2016-10; 
Priyanka A, Solanki V, Parkesh R, Thakur KG.
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Codon Optimization ... Cloning, overexpression and purification of MBP-SIRT7 NTD - The full-length codon optimized human sirt7 was synthesized commercially (GenScript). Among various constructs of SIRT7, only MBP-SIRT7 NTD produced diffraction quality crystals suitable for structural analyses. ... Get A Quote

摘要

Human SIRT7 is an NAD(+) dependent deacetylase, which belongs to sirtuin family of proteins. SIRT7, like other sirtuins has conserved catalytic domain and is flanked by N- and C-terminal domains reported to play vital functional roles. Here, we report the crystal structure of the N-terminal domain of human SIRT7 (SIRT7(NTD) ) at 2.3 Å resolution as MBP-SIRT7(NTD) fusion protein. SIRT7(NTD) adopts three-helical domain architecture and comparative structural analyses suggest similarities to some DNA binding motifs and transcription regulators. We also report here the importance of N- and C-terminal domains in soluble expression of SIRT7.

关键词

Human SIRT7; histone deacetylase; maltose binding protein; peptide mass fingerprinting; sirtuins; x-ray crystallography