1p9y

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Template:STRUCTURE 1p9y

Contents

Ribosome binding of E. coli Trigger Factor mutant F44L.

Template:ABSTRACT PUBMED 14656439

Function

[TIG_ECOLI] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity.[1] [2] [3]

About this Structure

1p9y is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA.

Reference

  • Kristensen O, Gajhede M. Chaperone binding at the ribosomal exit tunnel. Structure. 2003 Dec;11(12):1547-56. PMID:14656439
  1. ↑ Hesterkamp T, Hauser S, Lutcke H, Bukau B. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci U S A. 1996 Apr 30;93(9):4437-41. PMID:8633085
  2. ↑ Valent QA, Kendall DA, High S, Kusters R, Oudega B, Luirink J. Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J. 1995 Nov 15;14(22):5494-505. PMID:8521806
  3. ↑ Genevaux P, Keppel F, Schwager F, Langendijk-Genevaux PS, Hartl FU, Georgopoulos C. In vivo analysis of the overlapping functions of DnaK and trigger factor. EMBO Rep. 2004 Feb;5(2):195-200. Epub 2004 Jan 9. PMID:14726952 doi:10.1038/sj.embor.7400067

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