5I63

Crystal structure of TEM1 beta-lactamase mutant I263N in the presence of 1.2 MPa xenon

5I63 の概要

• エントリーDOI: 10.2210/pdb5i63/pdb
• 関連するPDBエントリー: 5I52
• 分子名称: Beta-lactamase TEM, XENON (3 entities in total)
• 機能のキーワード: hydrolase, xenon
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 116701.73

構造登録者

Roose, B.W.,Dmochowski, I.J. (登録日: 2016-02-15, 公開日: 2017-06-28, 最終更新日: 2024-11-13)

主引用文献

Roose, B.W.,Zemerov, S.D.,Wang, Y.,Kasimova, M.A.,Carnevale, V.,Dmochowski, I.J.
A Structural Basis for129Xe Hyper-CEST Signal in TEM-1 beta-Lactamase.
Chemphyschem, 2018

PubMed Abstract: Genetically encoded (GE) contrast agents detectable by magnetic resonance imaging (MRI) enable non-invasive visualization of gene expression and cell proliferation at virtually unlimited penetration depths. Using hyperpolarized Xe in combination with chemical exchange saturation transfer, an MR contrast approach known as hyper-CEST, enables ultrasensitive protein detection and biomolecular imaging. GE MRI contrast agents developed to date include nanoscale proteinaceous gas vesicles as well as the monomeric bacterial proteins TEM-1 β-lactamase (bla) and maltose binding protein (MBP). To improve understanding of hyper-CEST NMR with proteins, structural and computational studies were performed to further characterize the Xe-bla interaction. X-ray crystallography validated the location of a high-occupancy Xe binding site predicted by MD simulations, and mutagenesis experiments confirmed this Xe site as the origin of the observed CEST contrast. Structural studies and MD simulations with representative bla mutants offered additional insight regarding the relationship between local protein structure and CEST contrast.

PubMed: 30151973
DOI: 10.1002/cphc.201800624

実験手法

X-RAY DIFFRACTION (1.95 Å)