Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors

Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors The structure of the DNA‐binding NAC domain of Arabidopsis ANAC (abscisic‐acid‐responsive NAC) has been determined by X‐ray crystallography to 1.9 Å resolution (Protein Data Bank codes 1UT4 and 1UT7). This is the first structure determined for a member of the NAC family of plant‐specific transcriptional regulators. NAC proteins are characterized by their conserved N‐terminal NAC domains that can bind both DNA and other proteins. NAC proteins are involved in developmental processes, including formation of the shoot apical meristem, floral organs and lateral shoots, as well as in plant hormonal control and defence. The NAC domain does not possess a classical helix–turn–helix motif; instead it reveals a new transcription factor fold consisting of a twisted β‐sheet surrounded by a few helical elements. The functional dimer formed by the NAC domain was identified in the structure, which will serve as a structural template for understanding NAC protein function at the molecular level. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png EMBO Reports Wiley

Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors

Loading next page...
 
/lp/wiley/structure-of-the-conserved-domain-of-anac-a-member-of-the-nac-family-vBhY3s3Lxi

References (34)

Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
1469-221X
eISSN
1469-3178
DOI
10.1038/sj.embor.7400093
pmid
15083810
Publisher site
See Article on Publisher Site

Abstract

The structure of the DNA‐binding NAC domain of Arabidopsis ANAC (abscisic‐acid‐responsive NAC) has been determined by X‐ray crystallography to 1.9 Å resolution (Protein Data Bank codes 1UT4 and 1UT7). This is the first structure determined for a member of the NAC family of plant‐specific transcriptional regulators. NAC proteins are characterized by their conserved N‐terminal NAC domains that can bind both DNA and other proteins. NAC proteins are involved in developmental processes, including formation of the shoot apical meristem, floral organs and lateral shoots, as well as in plant hormonal control and defence. The NAC domain does not possess a classical helix–turn–helix motif; instead it reveals a new transcription factor fold consisting of a twisted β‐sheet surrounded by a few helical elements. The functional dimer formed by the NAC domain was identified in the structure, which will serve as a structural template for understanding NAC protein function at the molecular level.

Journal

EMBO ReportsWiley

Published: Mar 1, 2004

Keywords: ; ; ; ; ;

There are no references for this article.