TY  - JOUR
N1  - Open Access
ID  - open1897
UR  - http://onlinelibrary.wiley.com/doi/10.1002/prot.25085/abstract
IS  - 10
A1  - Priyanka, Anu
A1  - Solanki, Vipul
A1  - Parkesh, Raman
A1  - Thakur, Krishan Gopal
Y1  - 2016/10//
N2  - 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.
PB  - Wiley
JF  - Proteins
VL  - 84
KW  - Human SIRT7; histone deacetylase; maltose binding protein; peptide mass fingerprinting; sirtuins; x-ray crystallography
SN  - 1097-0134
TI  - Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture.
SP  - 1558
EP  - 63
ER  -