5AZ8
Crystal structure of MBP-Tom20 fusion protein tethered with ALDH presequence via a disulfide bond
5AZ8 の概要
| エントリーDOI | 10.2210/pdb5az8/pdb |
| 関連するPDBエントリー | 5AZ6 5AZ7 5AZ9 5AZA |
| 関連するBIRD辞書のPRD_ID | PRD_900001 |
| 分子名称 | Maltose-binding periplasmic protein,Mitochondrial import receptor subunit TOM20 homolog, peptide GPRLSRLLSYAGC, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total) |
| 機能のキーワード | fusion protein comlex, sugar binding protein, transport protein, peptide binding protein |
| 由来する生物種 | Escherichia coli (strain K12) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 49897.67 |
| 構造登録者 | |
| 主引用文献 | Matsuoka, R.,Shimada, A.,Komuro, Y.,Sugita, Y.,Kohda, D. Rational design of crystal contact-free space in protein crystals for analyzing spatial distribution of motions within protein molecules. Protein Sci., 25:754-768, 2016 Cited by PubMed Abstract: Contacts with neighboring molecules in protein crystals inevitably restrict the internal motions of intrinsically flexible proteins. The resultant clear electron densities permit model building, as crystallographic snapshot structures. Although these still images are informative, they could provide biased pictures of the protein motions. If the mobile parts are located at a site lacking direct contacts in rationally designed crystals, then the amplitude of the movements can be experimentally analyzed. We propose a fusion protein method, to create crystal contact-free space (CCFS) in protein crystals and to place the mobile parts in the CCFS. Conventional model building fails when large amplitude motions exist. In this study, the mobile parts appear as smeared electron densities in the CCFS, by suitable processing of the X-ray diffraction data. We applied the CCFS method to a highly mobile presequence peptide bound to the mitochondrial import receptor, Tom20, and a catalytically relevant flexible segment in the oligosaccharyltransferase, AglB. These two examples demonstrated the general applicability of the CCFS method to the analysis of the spatial distribution of motions within protein molecules. PubMed: 26694222DOI: 10.1002/pro.2867 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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