Periplasmic chaperones--new structural and functional insights.
Although chaperones exist in the periplasmic compartment of Gram-negative bacterial cells, how they function is not well understood. New intriguing functional insights are provided by the solved crystal structure of the periplasmic chaperone SurA.
Behrens
Susanne
S
Department of Molecular Genetics and Preparative Molecular Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen, Goettingen, Germany.
D001665:Binding Sites; D002352:Carrier Proteins; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry*; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D019897:Periplasm / Q000378:metabolism*; D017433:Protein Structure, Secondary
D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C490900:SurA protein, E coli; C098640:periplasmic peptidylprolyl cis-trans isomerase; D019696:Peptidylprolyl Isomerase