1Q4B

S65T Q80R Green Fluorescent Protein (GFP) pH 5.5

1Q4B の概要

• エントリーDOI: 10.2210/pdb1q4b/pdb
• 関連するPDBエントリー: 1Q4A 1Q4C 1Q4D 1Q4E 1Q73
• 分子名称: Green Fluorescent Protein (2 entities in total)
• 機能のキーワード: green fluorescent protein, gfp, fluorophore, chromophore, luminescent protein
• 由来する生物種: Aequorea victoria
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26945.38

構造登録者

Jain, R.K.,Ranganathan, R. (登録日: 2003-08-02, 公開日: 2004-02-03, 最終更新日: 2023-11-15)

主引用文献

Jain, R.K.,Ranganathan, R.
Local complexity of amino acid interactions in a protein core.
Proc.Natl.Acad.Sci.USA, 101:111-116, 2004

PubMed Abstract: Atomic resolution structures of proteins indicate that the core is typically well packed, suggesting a densely connected network of interactions between amino acid residues. The combinatorial complexity of energetic interactions in such a network could be enormous, a problem that limits our ability to relate structure and function. Here, we report a case study of the complexity of amino acid interactions in a localized region within the core of the GFP, a particularly stable and tightly packed molecule. Mutations at three sites within the chromophore-binding pocket display an overlapping pattern of conformational change and are thermodynamically coupled, seemingly consistent with the dense network model. However, crystallographic and energetic analyses of coupling between mutations paint a different picture; pairs of mutations couple through independent "hotspots" in the region of structural overlap. The data indicate that, even in highly stable proteins, the core contains sufficient plasticity in packing to uncouple high-order energetic interactions of residues, a property that is likely general in proteins.

PubMed: 14684834
DOI: 10.1073/pnas.2534352100

実験手法

X-RAY DIFFRACTION (1.48 Å)