9MEM

Anabaena Sensory Rhodopsin Structure Determination from Paramagnetic Relaxation Enhancement and NMR Restraints

9MEM の概要

• エントリーDOI: 10.2210/pdb9mem/pdb
• NMR情報: BMRB: 25290
• 分子名称: Bacteriorhodopsin, RETINAL (2 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Nostoc sp.; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27529.27

構造登録者

Vaz, R.F.,Brown, L.,Ladizhansky, V. (登録日: 2024-12-06, 公開日: 2025-04-16, 最終更新日: 2025-09-03)

主引用文献

Vaz, R.F.,Brown, L.S.,Ladizhansky, V.
Membrane protein structure determination from Paramagnetic Relaxation Enhancement and internuclear distance restraints.
J.Biomol.Nmr, 79:181-197, 2025

PubMed Abstract: Magic angle spinning nuclear magnetic resonance (MAS NMR) is well suited for the determination of protein structure. The key structural information is obtained in the form of spectral cross peaks between spatially close nuclear spins, but assigning these cross peaks unambiguously to unique spin pairs is often a tedious task because of spectral overlap. Here, we use a seven-helical membrane protein Anabaena Sensory Rhodopsin (ASR) as a model system to demonstrate that transverse Paramagnetic Relaxation Enhancements (PRE) extracted from 2D MAS NMR spectra could be used to obtain a protein structural model. Starting with near complete assignments (93%) of ASR residues, TALOS + predicted backbone dihedral angles and secondary structure restraints in the form of backbone hydrogen bonds are combined with PRE-based restraints and used to generate a coarse model. This model is subsequently utilized as a template reference to facilitate automated assignments of highly ambiguous internuclear correlations. The template is used in an iterative cross peak assignment process and is progressively improved through the inclusion of disambiguated restraints, thereby converging to a low root-mean-square-deviation structural model. In addition to improving structure calculation conversion, the inclusion of PREs also improves packing between helices within an alpha-helical bundle.

PubMed: 40156665
DOI: 10.1007/s10858-025-00467-w

実験手法

SOLID-STATE NMR