1ZIJ

GCN4-LEUCINE ZIPPER CORE MUTANT ASN16ABA IN THE TRIMERIC STATE

1ZIJ の概要

• エントリーDOI: 10.2210/pdb1zij/pdb
• 分子名称: GENERAL CONTROL PROTEIN GCN4 (2 entities in total)
• 機能のキーワード: leucine zipper, amino-acid biosynthesis, transcription regulation, activator, dna-binding, nuclear protein, coiled coil
• 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: 12008.11

構造登録者

Gonzalez Junior, L.,Brown, R.A.,Richardson, D.,Alber, T. (登録日: 1996-10-30, 公開日: 1997-07-07, 最終更新日: 2024-06-05)

主引用文献

Gonzalez Junior, L.,Brown, R.A.,Richardson, D.,Alber, T.
Crystal structures of a single coiled-coil peptide in two oligomeric states reveal the basis for structural polymorphism
Nat.Struct.Biol., 3:1002-1010, 1996

PubMed Abstract: Each protein sequence generally adopts a single native fold, but the sequence features that confer structural uniqueness are not well understood. To define the basis for structural heterogeneity, we determined the high resolution X-ray crystal structures of a single GCN4 leucine-zipper mutant (Asn 16 to aminobutyric acid) in both dimeric and trimeric coiled-coil conformations. The mutant sequence is accommodated in two distinct structures by forming similarly-shaped packing surfaces with different sets of atoms. The trimer structure, in comparison to a previously-characterized trimeric mutant with substitutions in eight core residues, shows that the twist of individual helices and the helix-helix crossing angles can vary significantly to produce the most favoured packing arrangement.

PubMed: 8946853
DOI: 10.1038/nsb1296-1002

実験手法

X-RAY DIFFRACTION (2 Å)