PMID:12429090

Citation	Bitto, E and McKay, DB (2002) Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 10:1489-98
Abstract	The SurA protein facilitates correct folding of outer membrane proteins in gram-negative bacteria. The sequence of Escherichia coli SurA presents four segments, two of which are peptidyl-prolyl isomerases (PPIases); the crystal structure reveals an asymmetric dumbbell, in which the amino-terminal, carboxy-terminal, and first PPIase segments of the sequence form a core structural module, and the second PPIase segment is a satellite domain tethered approximately 30 A from this module. The core module, which is implicated in membrane protein folding, has a novel fold that includes an extended crevice. Crystal contacts show that peptides bind within the crevice, suggesting a model for chaperone activity whereby segments of polypeptide may be repetitively sequestered and released during the membrane protein-folding process.
Links	PubMed
Keywords	Amino Acid Sequence; Binding Sites; Carrier Proteins; Cell Membrane/metabolism; Crystallography, X-Ray; Electrons; Escherichia coli/enzymology; Escherichia coli Proteins; Models, Molecular; Molecular Chaperones/chemistry; Molecular Sequence Data; Peptides/chemistry; Peptidylprolyl Isomerase/chemistry; Porins/chemistry; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Sequence Homology, Amino Acid
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