2LGI

Atomic Resolution Protein Structures using NMR Chemical Shift Tensors

2LGI の概要

• エントリーDOI: 10.2210/pdb2lgi/pdb
• 関連するPDBエントリー: 1GB1 1PGA 1PGB 2GB1 2GI9 2JSV 2JU6 2KOP 2KQ4 2KWD 2PLP 2QMT
• NMR情報: BMRB: 17810
• 分子名称: Immunoglobulin G-binding protein G (1 entity in total)
• 機能のキーワード: gb1, immunoglobulin binding domain, tedor, protein binding, igg-binding protein, peptidoglycan-anchor, secreted, thermostable
• 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: 1
• 化学式量合計: 6228.81

構造登録者

Wylie, B.J.,Sperling, L.J.,Nieuwkoop, A.J.,Franks, W.T.,Oldfield, E.,Rienstra, C.M. (登録日: 2011-07-26, 公開日: 2011-10-26, 最終更新日: 2024-05-01)

主引用文献

Wylie, B.J.,Sperling, L.J.,Nieuwkoop, A.J.,Franks, W.T.,Oldfield, E.,Rienstra, C.M.
Ultrahigh resolution protein structures using NMR chemical shift tensors.
Proc.Natl.Acad.Sci.USA, 108:16974-16979, 2011

PubMed Abstract: NMR chemical shift tensors (CSTs) in proteins, as well as their orientations, represent an important new restraint class for protein structure refinement and determination. Here, we present the first determination of both CST magnitudes and orientations for (13)Cα and (15)N (peptide backbone) groups in a protein, the β1 IgG binding domain of protein G from Streptococcus spp., GB1. Site-specific (13)Cα and (15)N CSTs were measured using synchronously evolved recoupling experiments in which (13)C and (15)N tensors were projected onto the (1)H-(13)C and (1)H-(15)N vectors, respectively, and onto the (15)N-(13)C vector in the case of (13)Cα. The orientations of the (13)Cα CSTs to the (1)H-(13)C and (13)C-(15)N vectors agreed well with the results of ab initio calculations, with an rmsd of approximately 8°. In addition, the measured (15)N tensors exhibited larger reduced anisotropies in α-helical versus β-sheet regions, with very limited variation (18 ± 4°) in the orientation of the z-axis of the (15)N CST with respect to the (1)H-(15)N vector. Incorporation of the (13)Cα CST restraints into structure calculations, in combination with isotropic chemical shifts, transferred echo double resonance (13)C-(15)N distances and vector angle restraints, improved the backbone rmsd to 0.16 Å (PDB ID code 2LGI) and is consistent with existing X-ray structures (0.51 Å agreement with PDB ID code 2QMT). These results demonstrate that chemical shift tensors have considerable utility in protein structure refinement, with the best structures comparable to 1.0-Å crystal structures, based upon empirical metrics such as Ramachandran geometries and χ(1)/χ(2) distributions, providing solid-state NMR with a powerful tool for de novo structure determination.

PubMed: 21969532
DOI: 10.1073/pnas.1103728108

実験手法

SOLID-STATE NMR