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Crystal structure of the N‐terminal domain of human SIRT7 reveals a three‐helical domain architecture
Author(s) -
Priyanka Anu,
Solanki Vipul,
Parkesh Raman,
Thakur Krishan Gopal
Publication year - 2016
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25085
Subject(s) - sirtuin , architecture domain , nad+ kinase , fusion protein , domain (mathematical analysis) , computational biology , microbiology and biotechnology , recombinant dna , chemistry , biology , genetics , architecture , biochemistry , gene , enzyme , art , mathematical analysis , mathematics , enterprise architecture management , visual arts , enterprise architecture
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.