2K9C

Paramagnetic shifts in solid-state NMR of Proteins to elicit structural information

2K9C の概要

• エントリーDOI: 10.2210/pdb2k9c/pdb
• 関連するPDBエントリー: 1RMZ
• 分子名称: Macrophage metalloelastase, COBALT (II) ION (2 entities in total)
• 機能のキーワード: matrix metalloproteinase, pseudocontact shift, paramagnetic nmr, hydrolase, calcium, extracellular matrix, glycoprotein, metal-binding, metalloprotease, polymorphism, protease, secreted, zinc, zymogen
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix (Probable): P39900
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16817.53

構造登録者

Balayssac, S.,Bertini, I.,Bhaumik, A.,Lelli, M.,Luchinat, C. (登録日: 2008-10-08, 公開日: 2008-11-18, 最終更新日: 2024-05-29)

主引用文献

Balayssac, S.,Bertini, I.,Bhaumik, A.,Lelli, M.,Luchinat, C.
Paramagnetic shifts in solid-state NMR of proteins to elicit structural information
Proc.Natl.Acad.Sci.Usa, 105:17284-17289, 2008

PubMed Abstract: The recent observation of pseudocontact shifts (pcs) in (13)C high-resolution solid-state NMR of paramagnetic proteins opens the way to their application as structural restraints. Here, by investigating a microcrystalline sample of cobalt(II)-substituted matrix metalloproteinase 12 [CoMMP-12 (159 AA, 17.5 kDa)], it is shown that a combined strategy of protein labeling and dilution of the paramagnetic species (i.e., (13)C-,(15)N-labeled CoMMP-12 diluted in unlabeled ZnMMP-12, and (13)C-,(15)N-labeled ZnMMP-12 diluted in unlabeled CoMMP-12) allows one to easily separate the pcs contributions originated from the protein internal metal (intramolecular pcs) from those due to the metals in neighboring proteins in the crystal lattice (intermolecular pcs) and that both can be used for structural purposes. It is demonstrated that intramolecular pcs are significant structural restraints helpful in increasing both precision and accuracy of the structure, which is a need in solid-state structural biology nowadays. Furthermore, intermolecular pcs provide unique information on positions and orientations of neighboring protein molecules in the solid phase.

PubMed: 18988744
DOI: 10.1073/pnas.0708460105

実験手法

SOLUTION NMR