1F43

SOLUTION STRUCTURE OF THE MATA1 HOMEODOMAIN

1F43 の概要

• エントリーDOI: 10.2210/pdb1f43/pdb
• 関連するPDBエントリー: 1YRN
• NMR情報: BMRB: 4637
• 分子名称: MATING-TYPE PROTEIN A-1 (1 entity in total)
• 機能のキーワード: homeodomain, helix-turn-helix, transcription
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7164.49

構造登録者

Anderson, J.S.,Forman, M.,Modleski, S.,Dahlquist, F.W.,Baxter, S.M. (登録日: 2000-06-07, 公開日: 2000-07-26, 最終更新日: 2024-05-22)

主引用文献

Anderson, J.S.,Forman, M.D.,Modleski, S.,Dahlquist, F.W.,Baxter, S.M.
Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain.
Biochemistry, 39:10045-10054, 2000

PubMed Abstract: The mating type homeodomain proteins, MATa1 and MATalpha2, combine to form a heterodimer to bind DNA in diploid yeast cells. The a1-alpha2 heterodimer tightly and specifically binds haploid-specific gene operators to repress transcription. On its own, however, the a1 homeodomain does not bind DNA in a sequence-specific manner. To help understand this interaction, we describe the solution structure and backbone dynamics of the free a1 homeodomain. Free a1 in solution is an ensemble of structures having flexible hinges at the two turns in the small protein fold. Conformational changes in the a1 homeodomain upon ternary complex formation are located in the loop between helix 1 and helix 2, where the C-terminal tail of alpha2 binds to form the heterodimer, and at the C-terminus of helix 3, the DNA recognition helix. The observed differences, comparing the free and bound a1 structures, suggest a mechanism linking van der Waals stacking changes to the ordering of a final turn in the DNA-binding helix of a1. The tail of alpha2 induces changes in loop 1 of a1 that push it toward a properly folded DNA binding conformation.

PubMed: 10955992
DOI: 10.1021/bi000677z

実験手法

SOLUTION NMR