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Folding of a synthetic parallel β‐roll protein
Author(s) -
Lilie Hauke,
Haehnel Wolfgang,
Rudolph Rainer,
Baumann Ulrich
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01308-9
Subject(s) - circular dichroism , chemistry , protein secondary structure , protein folding , beta sheet , peptide sequence , escherichia coli , structural motif , protein structure , stereochemistry , crystallography , biochemistry , gene
Recently, the design of β‐sheet proteins and concomitant folding studies have attracted increasing attention. A unique natural all‐β domain occurs in a family of cytolytic bacterial toxins, the so‐called RTX toxins. This domain consists of a variable number (about 6–45) of tandem repeats of a glycine‐rich nine‐residue motif with the consensus sequence GGXGXDX(L/I/F)X. The analysis of the three‐dimensional structure of alkaline protease from Pseudomonas aeruginosa which possesses six of these repeats revealed that they fold into a novel 'parallel β‐roll’ where calcium is bound within the turns connecting the β‐strands. A 75‐mer peptide of the sequence NH 2 ‐WLS‐[GGSGNDNLS] 8 ‐COOH was chemically synthesised. Circular dichroism spectroscopy showed that this polypeptide folds in the presence of Ca 2+ and polyethylene glycol into a β‐structure which is presumably identical with the parallel β‐roll. This synthetic β‐roll behaves similarly to the isolated β‐roll domains from Escherichia coli haemolysin or Bordetella pertussis cyclolysin in terms of calcium binding and polymerisation behaviour.