2A5M

NMR structure of murine gamma-S crystallin from joint refinement with SAXS data

2A5M の概要

• エントリーDOI: 10.2210/pdb2a5m/pdb
• 関連するPDBエントリー: 1A45 1A5D 1A7H 1AG4 1AMM 1HK0 1ZWM 1ZWO
• 分子名称: Gamma crystallin S (1 entity in total)
• 機能のキーワード: saxs, small-angle x-ray scattering, alignment, deuteration, liquid crystal, pf1, rdc, residual dipolar coupling, molecular fragment replacement, mfr, structural protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20747.27

構造登録者

Grishaev, A.,Wu, J.,Trewhella, J.,Bax, A. (登録日: 2005-06-30, 公開日: 2005-07-19, 最終更新日: 2024-05-22)

主引用文献

Grishaev, A.,Wu, J.,Trewhella, J.,Bax, A.
Refinement of Multidomain Protein Structures by Combination of Solution Small-Angle X-ray Scattering and NMR Data.
J.Am.Chem.Soc., 127:16621-16628, 2005

PubMed Abstract: Determination of the 3D structures of multidomain proteins by solution NMR methods presents a number of unique challenges related to their larger molecular size and the usual scarcity of constraints at the interdomain interface, often resulting in a decrease in structural accuracy. In this respect, experimental information from small-angle scattering of X-ray radiation in solution (SAXS) presents a suitable complement to the NMR data, as it provides an independent constraint on the overall molecular shape. A computational procedure is described that allows incorporation of such SAXS data into the mainstream high-resolution macromolecular structure refinement. The method is illustrated for a two-domain 177-amino-acid protein, gammaS crystallin, using an experimental SAXS data set fitted at resolutions from approximately 200 A to approximately 30 A. Inclusion of these data during structure refinement decreases the backbone coordinate root-mean-square difference between the derived model and the high-resolution crystal structure of a 54% homologous gammaB crystallin from 1.96 +/- 0.07 A to 1.31 +/- 0.04 A. Combining SAXS data with NMR restraints can be accomplished at a moderate computational expense and is expected to become useful for multidomain proteins, multimeric assemblies, and tight macromolecular complexes.

PubMed: 16305251
DOI: 10.1021/ja054342m

実験手法

SOLUTION NMR