2KS6

NMR solution structure of ALG13 --- obtained with iterative CS-Rosetta from backbone NMR data.

2KS6 の概要

• エントリーDOI: 10.2210/pdb2ks6/pdb
• 関連するPDBエントリー: 2jzc
• 分子名称: UDP-N-acetylglucosamine transferase subunit ALG13 (1 entity in total)
• 機能のキーワード: cs-rosetta, cyclic n-oxides, endoplasmic reticulum, glycosyltransferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Endoplasmic reticulum: P53178
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22552.82

構造登録者

Lange, O.F.,Wang, X.,Prestegard, J.H.,Baker, D. (登録日: 2009-12-29, 公開日: 2011-01-12, 最終更新日: 2024-05-01)

主引用文献

Raman, S.,Lange, O.F.,Rossi, P.,Tyka, M.,Wang, X.,Aramini, J.,Liu, G.,Ramelot, T.A.,Eletsky, A.,Szyperski, T.,Kennedy, M.A.,Prestegard, J.,Montelione, G.T.,Baker, D.
NMR structure determination for larger proteins using backbone-only data.
Science, 327:1014-1018, 2010

PubMed Abstract: Conventional protein structure determination from nuclear magnetic resonance data relies heavily on side-chain proton-to-proton distances. The necessary side-chain resonance assignment, however, is labor intensive and prone to error. Here we show that structures can be accurately determined without nuclear magnetic resonance (NMR) information on the side chains for proteins up to 25 kilodaltons by incorporating backbone chemical shifts, residual dipolar couplings, and amide proton distances into the Rosetta protein structure modeling methodology. These data, which are too sparse for conventional methods, serve only to guide conformational search toward the lowest-energy conformations in the folding landscape; the details of the computed models are determined by the physical chemistry implicit in the Rosetta all-atom energy function. The new method is not hindered by the deuteration required to suppress nuclear relaxation processes for proteins greater than 15 kilodaltons and should enable routine NMR structure determination for larger proteins.

PubMed: 20133520
DOI: 10.1126/science.1183649

実験手法

SOLUTION NMR