1UT4

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

Summary for 1UT4

• Entry DOI: 10.2210/pdb1ut4/pdb
• Related: 1UT7
• Descriptor: NO APICAL MERISTEM PROTEIN (2 entities in total)
• Functional Keywords: transcription regulation, transcription, transcription factor, dna binding, abscisic acid response, arabidopsis thaliana, nac domain
• Biological source: ARABIDOPSIS THALIANA (MOUSE-EAR CRESS)
• Cellular location: Nucleus : Q9C932
• Total number of polymer chains: 2
• Total formula weight: 39561.33

Authors

Ernst, H.A.,Olsen, A.N.,Skriver, K.,Larsen, S.,Lo Leggio, L. (deposition date: 2003-12-03, release date: 2004-03-19, Last modification date: 2024-05-08)

Primary citation

Ernst, H.A.,Olsen, A.N.,Skriver, K.,Larsen, S.,Lo Leggio, L.
Structure of the Conserved Domain of Anac, a Member of the Nac Family of Transcription Factors
Embo Rep., 5:297-, 2004

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

PubMed: 15083810
DOI: 10.1038/SJ.EMBOR.7400093

Experimental method

X-RAY DIFFRACTION (2.5 Å)