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2MLX

NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310

Summary for 2MLX
Entry DOI10.2210/pdb2mlx/pdb
Related2mly 2mlz
NMR InformationBMRB: 19835
DescriptorTrigger factor, Alkaline phosphatase (2 entities in total)
Functional Keywordsmolecular chaperone, unfolded protein, protein complex, chaperone
Biological sourceEscherichia coli
More
Cellular locationCytoplasm: U6N3P1
Total number of polymer chains2
Total formula weight59562.24
Authors
Saio, T.,Guan, X.,Rossi, P.,Economou, A.,Kalodimos, C.G. (deposition date: 2014-03-05, release date: 2014-05-21, Last modification date: 2024-05-01)
Primary citationSaio, T.,Guan, X.,Rossi, P.,Economou, A.,Kalodimos, C.G.
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Science, 344:1250494-1250494, 2014
Cited by
PubMed Abstract: Molecular chaperones prevent aggregation and misfolding of proteins, but scarcity of structural data has impeded an understanding of the recognition and antiaggregation mechanisms. We report the solution structure, dynamics, and energetics of three trigger factor (TF) chaperone molecules in complex with alkaline phosphatase (PhoA) captured in the unfolded state. Our data show that TF uses multiple sites to bind to several regions of the PhoA substrate protein primarily through hydrophobic contacts. Nuclear magnetic resonance (NMR) relaxation experiments show that TF interacts with PhoA in a highly dynamic fashion, but as the number and length of the PhoA regions engaged by TF increase, a more stable complex gradually emerges. Multivalent binding keeps the substrate protein in an extended, unfolded conformation. The results show how molecular chaperones recognize unfolded polypeptides and, by acting as unfoldases and holdases, prevent the aggregation and premature (mis)folding of unfolded proteins.
PubMed: 24812405
DOI: 10.1126/science.1250494
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

227933

數據於2024-11-27公開中

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