2M66

Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: 3D Protein Fold Determination from Backbone Amide Pseudocontact Shifts Generated by Lanthanide Tags at Multiple Sites

2M66 の概要

• エントリーDOI: 10.2210/pdb2m66/pdb
• 関連するPDBエントリー: 1G7D
• NMR情報: BMRB: 4920
• 分子名称: Endoplasmic reticulum resident protein 29 (1 entity in total)
• 機能のキーワード: erp29, erp29-c, chaperone, gps-rosetta
• 由来する生物種: Rattus norvegicus (Rat)
• 細胞内の位置: Endoplasmic reticulum lumen: P52555
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11787.47

構造登録者

Yagi, H.,Pilla, K.,Maleckis, A.,Graham, B.,Huber, T.,Otting, G. (登録日: 2013-03-26, 公開日: 2013-07-10, 最終更新日: 2024-05-01)

主引用文献

Yagi, H.,Pilla, K.B.,Maleckis, A.,Graham, B.,Huber, T.,Otting, G.
Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites
Structure, 21:883-890, 2013

PubMed Abstract: Site-specific attachment of paramagnetic lanthanide ions to a protein generates pseudocontact shifts (PCS) in the nuclear magnetic resonance (NMR) spectra of the protein that are easily measured as changes in chemical shifts. By labeling the protein with lanthanide tags at four different sites, PCSs are observed for most amide protons and accurate information is obtained about their coordinates in three-dimensional space. The approach is demonstrated with the chaperone ERp29, for which large differences have been reported between X-ray and NMR structures of the C-terminal domain, ERp29-C. The results unambiguously show that the structure of rat ERp29-C in solution is similar to the crystal structure of human ERp29-C. PCSs of backbone amides were the only structural restraints required. Because these can be measured for more dilute protein solutions than other NMR restraints, the approach greatly widens the range of proteins amenable to structural studies in solution.

PubMed: 23643949
DOI: 10.1016/j.str.2013.04.001

実験手法

SOLUTION NMR