1MPE

Ensemble of 20 structures of the tetrameric mutant of the B1 domain of streptococcal protein G

1MPE の概要

• エントリーDOI: 10.2210/pdb1mpe/pdb
• 関連するPDBエントリー: 1GB1
• NMR情報: BMRB: 5654
• 分子名称: Immunoglobulin G binding protein G (1 entity in total)
• 機能のキーワード: strand-exchanged tetramer, channel, protein binding
• 由来する生物種: Streptococcus sp. 'group G'
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): P06654
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 25211.72

構造登録者

Frank, M.K.,Dyda, F.,Dobrodumov, A.,Gronenborn, A.M. (登録日: 2002-09-12, 公開日: 2002-10-30, 最終更新日: 2024-05-22)

主引用文献

Kirsten Frank, M.,Dyda, F.,Dobrodumov, A.,Gronenborn, A.M.
Core mutations switch monomeric protein GB1 into an intertwined tetramer.
Nat.Struct.Biol., 9:877-885, 2002

PubMed Abstract: The structure of a mutant immunoglobulin-binding B1 domain of streptococcal protein G (GB1), which comprises five conservative changes in hydrophobic core residues, was determined by NMR spectroscopy and X-ray crystallography. The oligomeric state and quaternary structure of the mutant protein are drastically changed from the wild type protein. The mutant structure consists of a symmetric tetramer, with intermolecular strand exchange involving all four units. Four of the five secondary structure elements present in the monomeric wild type GB1 structure are retained in the tetrameric structure, although their intra- and intermolecular interactions are altered. Our results demonstrate that through the acquisition of a moderate number of pivotal point mutations, proteins such as GB1 are able to undergo drastic structural changes, overcoming reduced stability of the monomeric unit by multimerization. The present structure is an illustrative example of how proteins exploit the breadth of conformational space.

PubMed: 12379842
DOI: 10.1038/nsb854

実験手法

SOLUTION NMR