1DU0

ENGRAILED HOMEODOMAIN Q50A VARIANT DNA COMPLEX

1DU0 の概要

• エントリーDOI: 10.2210/pdb1du0/pdb
• 関連するPDBエントリー: 1HDD 2HDD 3HDD
• 分子名称: DNA (5'-D(*TP*TP*TP*TP*GP*CP*CP*AP*TP*GP*TP*AP*AP*TP*TP*AP*CP*CP*TP*AP*A)-3'), DNA (5'-D(*AP*TP*TP*AP*GP*GP*TP*AP*AP*TP*TP*AP*CP*AP*TP*GP*GP*CP*AP*AP*A)-3'), ENGRAILED HOMEODOMAIN, ... (4 entities in total)
• 機能のキーワード: homeodomain, dna-binding protein, protein-dna complex, transcription-dna complex, transcription/dna
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Nucleus: P02836
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 26697.25

構造登録者

Grant, R.A.,Rould, M.A.,Klemm, J.D.,Pabo, C.O. (登録日: 2000-01-13, 公開日: 2000-07-31, 最終更新日: 2024-02-07)

主引用文献

Grant, R.A.,Rould, M.A.,Klemm, J.D.,Pabo, C.O.
Exploring the role of glutamine 50 in the homeodomain-DNA interface: crystal structure of engrailed (Gln50 --> ala) complex at 2.0 A.
Biochemistry, 39:8187-8192, 2000

PubMed Abstract: We have determined the crystal structure of a complex containing the engrailed homeodomain Gln50 --> Ala variant (QA50) bound to the wild-type optimal DNA site (TAATTA) at 2.0 A resolution. Biochemical and genetic studies by other groups have suggested that residue 50 is an important determinant of differential DNA-binding specificity among homeodomains (distinguishing among various sites of the general form TAATNN). However, biochemical studies of the QA50 variant had revealed that it binds almost as tightly as the wild-type protein and with only modest changes in specificity. We have now determined the crystal structure of the QA50 variant to help understand the role of residue 50 in site-specific recognition. Our cocrystal structure shows some interesting changes in the water structure at the site of the substitution and shows some changes in the conformations of neighboring side chains. However, the structure, like the QA50 biochemical data, suggests that Gln50 plays a relatively modest role in determining the affinity and specificity of the engrailed homeodomain.

PubMed: 10889025
DOI: 10.1021/bi000071a

実験手法

X-RAY DIFFRACTION (2 Å)