1MH4

maltose binding-a1 homeodomain protein chimera, crystal form II

1MH4 の概要

• エントリーDOI: 10.2210/pdb1mh4/pdb
• 関連するPDBエントリー: 1MH3
• 分子名称: maltose binding-a1 homeodomain protein chimera (2 entities in total)
• 機能のキーワード: mata1, homeodomain, binding cooperativity, maltose binding protein, mbp, sugar binding, dna binding protein
• 由来する生物種: Escherichia coli (, baker's yeast); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46403.83

構造登録者

Ke, A.,Wolberger, C. (登録日: 2002-08-19, 公開日: 2002-09-18, 最終更新日: 2024-02-14)

主引用文献

Ke, A.,Wolberger, C.
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera
Protein Sci., 12:306-312, 2003

PubMed Abstract: The Yeast MATa1 and MATalpha2 are homeodomain proteins that bind DNA cooperatively to repress transcription of cell type specific genes. The DNA affinity and specificity of MATa1 in the absence of MATalpha2, however, is very low. MATa1 is converted to a higher affinity DNA-binding protein by its interaction with the C-terminal tail of MATalpha2. To understand why MATa1 binds DNA weakly by itself, and how the MATalpha2 tail affects the affinity of MATa1 for DNA, we determined the crystal structure of a maltose-binding protein (MBP)-a1 chimera whose DNA binding behavior is similar to MATa1. The overall MATa1 conformation in the MBP-a1 structure, which was determined in the absence of alpha2 and DNA, is similar to that in the a1/alpha2/DNA structure. The sole difference is in the C-terminal portion of the DNA recognition helix of MATa1, which is flexible in the present structure. However, these residues are not in a location likely to be affected by binding of the MATalpha2 tail. The results argue against conformational changes in a1 induced by the tail of MATalpha2, suggesting instead that the MATalpha2 tail energetically couples the DNA binding of MATalpha2 and MATa1.

PubMed: 12538894
DOI: 10.1110/ps.0219103

実験手法

X-RAY DIFFRACTION (2.3 Å)