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5B3Z

Crystal structure of hPin1 WW domain (5-39) fused with maltose-binding protein

Summary for 5B3Z
Entry DOI10.2210/pdb5b3z/pdb
Related5B3W 5B3X 5B3Y
Related PRD IDPRD_900001
DescriptorPeptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Maltose-binding periplasmic protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
Functional Keywordsisomerase, sugar binding protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight179926.84
Authors
Hanazono, Y.,Takeda, K.,Miki, K. (deposition date: 2016-03-17, release date: 2016-10-26, Last modification date: 2023-11-08)
Primary citationHanazono, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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