5BMY

Crystal structure of hPin1 WW domain (5-21) fused with maltose-binding protein

Summary for 5BMY

• Entry DOI: 10.2210/pdb5bmy/pdb
• Related PRD ID: PRD_900001
• Descriptor: Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Maltose-binding periplasmic protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: ww domain, maltose-binding protein, sugar binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 1
• Total formula weight: 43160.78

Authors

Hanazono, Y.,Takeda, K.,Miki, K. (deposition date: 2015-05-25, release date: 2016-10-26, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.001 Å)