5B3X

Crystal structure of hPin1 WW domain (5-15) fused with maltose-binding protein in P41212 form

5B3X の概要

• エントリーDOI: 10.2210/pdb5b3x/pdb
• 関連するPDBエントリー: 5B3W 5B3Y 5B3Z
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Maltose-binding periplasmic protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: isomerase, sugar binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42396.91

構造登録者

Hanazono, Y.,Takeda, K.,Miki, K. (登録日: 2016-03-17, 公開日: 2016-10-26, 最終更新日: 2023-11-08)

主引用文献

Hanazono, Y.,Takeda, K.,Miki, K.
Structural studies of the N-terminal fragments of the WW domain: Insights into co-translational folding of a beta-sheet protein
Sci Rep, 6:34654-34654, 2016

PubMed Abstract: Nascent proteins fold co-translationally because the folding speed and folding pathways are limited by the rate of ribosome biosynthesis in the living cell. In addition, though full-length proteins can fold all their residues during the folding process, nascent proteins initially fold only with the N-terminal residues. However, the transient structure and the co-translational folding pathway are not well understood. Here we report the atomic structures of a series of N-terminal fragments of the WW domain with increasing amino acid length. Unexpectedly, the structures indicate that the intermediate-length fragments take helical conformations even though the full-length protein has no helical regions. The circular dichroism spectra and theoretical calculations also support the crystallographic results. This suggests that the short-range interactions are more decisive in the structure formation than the long-range interactions for short nascent proteins. In the course of the peptide extension, the helical structure change to the structure mediated by the long-range interactions at a particular polypeptide length. Our results will provide unique information for elucidating the nature of co-translational folding.

PubMed: 27698466
DOI: 10.1038/srep34654

実験手法

X-RAY DIFFRACTION (2.4 Å)