1ut7

From Proteopedia

Revision as of 15:05, 5 November 2007

STRUCTURE OF THE CONSERVED DOMAIN OF ANAC, A MEMBER OF THE NAC FAMILY OF TRANSCRIPTION FACTORS

Overview

The structure of the DNA-binding NAC domain of Arabidopsis ANAC, (abscisic-acid-responsive NAC) has been determined by X-ray, crystallography to 1.9A 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 beta-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.

About this Structure

1UT7 is a Single protein structure of sequence from Arabidopsis thaliana with AU as ligand. Structure known Active Site: AC3. Full crystallographic information is available from OCA.

Reference

Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors., Ernst HA, Olsen AN, Larsen S, Lo Leggio L, EMBO Rep. 2004 Mar;5(3):297-303. PMID:15083810

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