SurA

SurA is a molecular chaperone that is localized in the periplasm of gram-negative bacteria. It is thought to facilitate correct folding/assembly of outer membrane porins. Although sequence analysis shows that SurA has two peptidyl-prolyl isomerase domains, these are not essential for biological activity; however, the non-prolyl-isomerase domains of the sequence are essential. The structure is bipartite; a core domain has an extended, deep cleft, and one prolyl-isomerase domain is tethered ~30 Angstroms from this core. Peptide studies reveal that SurA recognizes an Aromatic-X-Aromatic sequence motif, which is characteristic of the "aromatic bands" of outer membrane porins. The mechanism by which SurA chaperones protein folding remains unclear.

SurA

Publications

E. Bitto & D. B. McKay
"Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins"
Structure 10, 1489-1498 (2002).
[PubMed] [SurA coordinates]

E. Bitto & D. B. McKay
"The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins"
J. Biol. Chem. 278, 49316-49322 (2003).
[PubMed]

E. Bitto & D. B. McKay
"Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins"
FEBS Letters 568, 94-98 (2004).
[PubMed]

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