1GCM

GCN4 LEUCINE ZIPPER CORE MUTANT P-LI

1GCM の概要

• エントリーDOI: 10.2210/pdb1gcm/pdb
• 分子名称: GCN4P-II (2 entities in total)
• 機能のキーワード: hydrophobic core mutant, transcription regulation
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P03069
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 12218.51

構造登録者

Harbury, P.B.,Kim, P.S.,Alber, T. (登録日: 1995-04-25, 公開日: 1996-01-29, 最終更新日: 2024-11-13)

主引用文献

Harbury, P.B.,Kim, P.S.,Alber, T.
Crystal structure of an isoleucine-zipper trimer.
Nature, 371:80-83, 1994

PubMed Abstract: Subunit oligomerization in many proteins is mediated by short coiled-coil motifs. These motifs share a characteristic seven-amino-acid repeat containing hydrophobic residues at the first (a) and fourth (d) positions. Despite this common pattern, different sequences form two-, three- and four-stranded helical ropes. We have investigated the basis for oligomer choice by characterizing variants of the GCN4 leucine-zipper dimerization domain that adopt trimeric or tetrameric structures in response to mutations at the a and d positions. We now report the high-resolution X-ray crystal structure of an isoleucine-containing mutant that folds into a parallel three-stranded, alpha-helical coiled coil. In contrast to the dimer and tetramer structures, the interior packing of the trimer can accommodate beta-branched residues in the most preferred rotamer at both hydrophobic positions. Compatibility of the shape of the core amino acids with the distinct packing spaces in the two-, three- and four-stranded conformations appears to determine the oligomerization state of the GCN4 leucine-zipper variants.

PubMed: 8072533
DOI: 10.1038/371080a0

実験手法

X-RAY DIFFRACTION (1.8 Å)