1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli

Volume: 13, Issue: 1, Pages: 183 - 186
Published: Jan 25, 2019
Abstract
The periplasmic chaperone SurA in Gram-negative bacteria plays a central role in the biogenesis of integral outer membrane proteins and is critical to the maintenance of bacterial membrane integrity. SurA contains a core chaperone module comprising the N- and C-terminal domains, along with two peptidyl-prolyl isomerase (PPIase) domains. The chaperone activity of SurA has been demonstrated to rely on the core module, whereas recent works...
Paper Details
Title
1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli
Published Date
Jan 25, 2019
Volume
13
Issue
1
Pages
183 - 186
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