2HM4

Nematocyst Outer Wall Antigen, NW1 K21P

2HM4 の概要

• エントリーDOI: 10.2210/pdb2hm4/pdb
• 関連するPDBエントリー: 2HM3
• 分子名称: Nematocyst outer wall antigen (1 entity in total)
• 機能のキーワード: evolution, cysteine rich, nematocyst, structural protein
• 由来する生物種: Hydra vulgaris
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3048.37

構造登録者

Meier, S.,Jensen, P.R.,Grzesiek, S.,Oezbek, S. (登録日: 2006-07-11, 公開日: 2007-02-06, 最終更新日: 2024-10-30)

主引用文献

Meier, S.,Jensen, P.R.,David, C.N.,Chapman, J.,Holstein, T.W.,Grzesiek, S.,Ozbek, S.
Continuous molecular evolution of protein-domain structures by single amino Acid changes.
Curr.Biol., 17:173-178, 2007

PubMed Abstract: Protein structures cluster into families of folds that can result from extremely different amino acid sequences [1]. Because the enormous amount of genetic information generates a limited number of protein folds [2], a particular domain structure often assumes numerous functions. How new protein structures and new functions evolve under these limitations remains elusive. Molecular evolution may be driven by the ability of biomacromolecules to adopt multiple conformations as a bridge between different folds [3-6]. This could allow proteins to explore new structures and new tasks while part of the structural ensemble retains the initial conformation and function as a safeguard [7]. Here we show that a global structural switch can arise from single amino acid changes in cysteine-rich domains (CRD) of cnidarian nematocyst proteins. The ability of these CRDs to form two structures with different disulfide patterns from an identical cysteine pattern is distinctive [8]. By applying a structure-based mutagenesis approach, we demonstrate that a cysteine-rich domain can interconvert between two natively occurring domain structures via a bridge state containing both structures. Comparing cnidarian CRD sequences leads us to believe that the mutations we introduced to stabilize each structure reflect the birth of new protein folds in evolution.

PubMed: 17240343
DOI: 10.1016/j.cub.2006.10.063

実験手法

SOLUTION NMR