1AJY

STRUCTURE AND MOBILITY OF THE PUT3 DIMER: A DNA PINCER, NMR, 13 STRUCTURES

1AJY の概要

• エントリーDOI: 10.2210/pdb1ajy/pdb
• 分子名称: PUT3, ZINC ION (2 entities in total)
• 機能のキーワード: transcription regulation, put3
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P25502
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16450.69

構造登録者

Walters, K.J.,Dayie, K.T.,Reece, R.J.,Ptashne, M.,Wagner, G. (登録日: 1997-05-12, 公開日: 1997-09-17, 最終更新日: 2024-05-22)

主引用文献

Walters, K.J.,Dayie, K.T.,Reece, R.J.,Ptashne, M.,Wagner, G.
Structure and mobility of the PUT3 dimer.
Nat.Struct.Biol., 4:744-750, 1997

PubMed Abstract: The solution structure and backbone dynamics of the transcriptional activator PUT3 (31-100) has been characterized using NMR spectroscopy. PUT3 (31-100) contains three distinct domains: a cysteine zinc cluster, linker, and dimerization domain. The cysteine zinc cluster of PUT3 closely resembles the solution structure of GAL4, while the dimerization domain forms a long coiled-coil similar to that observed in the crystal structures of GAL4 and PPR1. However, the residues at the N-terminal end of the coiled-coil behave very differently in each of these proteins. A comparison of the structural elements within this region provides a model for the DNA binding specificity of these proteins. Furthermore, we have characterized the dynamics of PUT3 to find that the zinc cluster and dimerization domains have very diverse dynamics in solution. The dimerization domain behaves as a large protein, while the peripheral cysteine zinc clusters have dynamic properties similar to small proteins.

PubMed: 9303003
DOI: 10.1038/nsb0997-744

実験手法

SOLUTION NMR