The disordered mobile loop of GroES folds into a defined beta-hairpin upon binding GroEL.
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.
Shewmaker
F
F
Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, Louisiana 70112-2699, USA.
Maskos
K
K
Simmerling
C
C
Landry
S J
SJ
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
D001426:Bacterial Proteins; D018835:Chaperonin 10; C097970:GroESL protein, Bacteria; D018833:Chaperonins