2mly | pdb_00002mly

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NMR structure of E. coli Trigger Factor in complex with unfolded PhoA1-150

spinqualitylabelsall models 2mly, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mly is a 2 chain structure with sequence from Escherichia coli str. k-12 substr. mc4100. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2mlx, 2mlz Gene: tig, BN896_0318 (Escherichia coli str. K-12 substr. MC4100), phoA, BN896_0267 (Escherichia coli str. K-12 substr. MC4100) Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [U6N325_ECOLI] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation (By similarity).[RuleBase:RU003914] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).[HAMAP-Rule:MF_00303] Publication Abstract from PubMed 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. Structural basis for protein antiaggregation activity of the trigger factor chaperone.,Saio T, Guan X, Rossi P, Economou A, Kalodimos CG Science. 2014 May 9;344(6184):1250494. doi: 10.1126/science.1250494. PMID:24812405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alkaline phosphatase

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