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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Nat+Struct+Mol+Biol
2016 ; 23
(7
): 691-7
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Visualizing chaperone-assisted protein folding
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Horowitz S
; Salmon L
; Koldewey P
; Ahlstrom LS
; Martin R
; Quan S
; Afonine PV
; van den Bedem H
; Wang L
; Xu Q
; Trievel RC
; Brooks CL 3rd
; Bardwell JC
Nat Struct Mol Biol
2016[Jul]; 23
(7
): 691-7
PMID27239796
show ga
Challenges in determining the structures of heterogeneous and dynamic protein
complexes have greatly hampered past efforts to obtain a mechanistic
understanding of many important biological processes. One such process is
chaperone-assisted protein folding. Obtaining structural ensembles of
chaperone-substrate complexes would ultimately reveal how chaperones help
proteins fold into their native state. To address this problem, we devised a new
structural biology approach based on X-ray crystallography, termed residual
electron and anomalous density (READ). READ enabled us to visualize even sparsely
populated conformations of the substrate protein immunity protein 7 (Im7) in
complex with the Escherichia coli chaperone Spy, and to capture a series of
snapshots depicting the various folding states of Im7 bound to Spy. The ensemble
shows that Spy-associated Im7 samples conformations ranging from unfolded to
partially folded to native-like states and reveals how a substrate can explore
its folding landscape while being bound to a chaperone.
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