1ut7: Difference between revisions

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==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.

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==

Line 13:

[[Category: Arabidopsis thaliana]]

[[Category: Single protein]]

[[Category: Ernst, H.A.]]

[[Category: Ernst, H A.]]

[[Category: Larsen, S.]]

[[Category: Leggio, L.Lo.]]

[[Category: Leggio, L Lo.]]

[[Category: Olsen, A.N.]]

[[Category: Olsen, A N.]]

[[Category: Skriver, K.]]

[[Category: AU]]

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[[Category: transcription factor]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 13: / Line 13: @@
 [[Category: Arabidopsis thaliana]]
 [[Category: Single protein]]
-[[Category: Ernst, H.A.]]
+[[Category: Ernst, H A.]]
 [[Category: Larsen, S.]]
-[[Category: Leggio, L.Lo.]]
+[[Category: Leggio, L Lo.]]
-[[Category: Olsen, A.N.]]
+[[Category: Olsen, A N.]]
 [[Category: Skriver, K.]]
 [[Category: AU]]
@@ Line 27: / Line 27: @@
 [[Category: transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:04:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:03 2008''