%0 Journal Article
%@ 1097-0134
%A Priyanka, Anu
%A Solanki, Vipul
%A Parkesh, Raman
%A Thakur, Krishan Gopal
%D 2016
%F open:1897
%I Wiley
%J Proteins
%K Human SIRT7; histone deacetylase; maltose binding protein; peptide mass fingerprinting; sirtuins; x-ray crystallography
%N 10
%P 1558-63
%T Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture.
%U http://crdd.osdd.net/open/1897/
%V 84
%X 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. Proteins 2016; 84:1558-1563. © 2016 Wiley Periodicals, Inc.
%Z Open Access