| Literature DB >> 27287224 |
Anu Priyanka1, Vipul Solanki1, Raman Parkesh2, Krishan Gopal Thakur3.
Abstract
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.Entities:
Keywords: Human SIRT7; histone deacetylase; maltose binding protein; peptide mass fingerprinting; sirtuins; x-ray crystallography
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Year: 2016 PMID: 27287224 DOI: 10.1002/prot.25085
Source DB: PubMed Journal: Proteins ISSN: 0887-3585