title: The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL.
abstract: The GroES mobile loop is a stretch of approximately 16 amino acids that exhibits a high degree of flexible disorder in the free protein. This loop is responsible for the interaction between GroES and GroEL, and it undergoes a folding transition upon binding to GroEL. Results derived from a combination of transferred nuclear Overhauser effect NMR experiments and molecular dynamics simulations indicate that the mobile loop adopts a beta-hairpin structure with a Type I, G1 Bulge turn. This structure is distinct from the conformation of the loop in the co-crystal of GroES with GroEL-ADP but identical to the conformation of the bacteriophage-panned "strongly binding peptide" in the co-crystal with GroEL. Analysis of sequence conservation suggests that sequences of the mobile loop and strongly binding peptide were selected for the ability to adopt this hairpin conformation.
authors.affiliation: Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, USA.
authors.forename: F
authors.initials: F
authors.lastname: Shewmaker
authors.forename: K
authors.initials: K
authors.lastname: Maskos
authors.forename: C
authors.initials: C
authors.lastname: Simmerling
authors.forename: S J
authors.initials: SJ
authors.lastname: Landry
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D018835:Chaperonin 10 / Q000737:chemistry*; D018833:Chaperonins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D001426:Bacterial Proteins; D018835:Chaperonin 10; C097970:GroESL protein, Bacteria; D018833:Chaperonins