1S0W

1b Lactamse/ b Lactamase Inhibitor

1S0W の概要

• エントリーDOI: 10.2210/pdb1s0w/pdb
• 関連するPDBエントリー: 1jtg
• 分子名称: beta-lactamase TEM, Beta-lactamase inhibitory protein, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: protein-protein complex, tem-1 beta-lactamase, beta-lactamase inhibitor protein, blip, israel structural proteomics center, ispc, structural genomics, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Secreted: P00810
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 92924.94

構造登録者

Schreiber, G.,Reichman, D.,Israel Structural Proteomics Center (ISPC) (登録日: 2004-01-05, 公開日: 2004-02-10, 最終更新日: 2024-11-20)

主引用文献

Reichmann, D.,Rahat, O.,Albeck, S.,Meged, R.,Dym, O.,Schreiber, G.
The modular architecture of protein-protein binding interfaces.
Proc.Natl.Acad.Sci.USA, 102:57-62, 2005

PubMed Abstract: Protein-protein interactions are essential for life. Yet, our understanding of the general principles governing binding is not complete. In the present study, we show that the interface between proteins is built in a modular fashion; each module is comprised of a number of closely interacting residues, with few interactions between the modules. The boundaries between modules are defined by clustering the contact map of the interface. We show that mutations in one module do not affect residues located in a neighboring module. As a result, the structural and energetic consequences of the deletion of entire modules are surprisingly small. To the contrary, within their module, mutations cause complex energetic and structural consequences. Experimentally, this phenomenon is shown on the interaction between TEM1-beta-lactamase and beta-lactamase inhibitor protein (BLIP) by using multiple-mutant analysis and x-ray crystallography. Replacing an entire module of five interface residues with Ala created a large cavity in the interface, with no effect on the detailed structure of the remaining interface. The modular architecture of binding sites, which resembles human engineering design, greatly simplifies the design of new protein interactions and provides a feasible view of how these interactions evolved.

PubMed: 15618400
DOI: 10.1073/pnas.0407280102

実験手法

X-RAY DIFFRACTION (2.3 Å)