The role of the disulfide bond in amyloid-like fibrillogenesis in a model peptide system

2005 ◽  
Vol 3 (19) ◽  
pp. 3502 ◽  
Author(s):  
Apurba Kumar Das ◽  
Michael G. B. Drew ◽  
Debasish Haldar ◽  
Arindam Banerjee
Keyword(s):  
Disulfide Bond ◽  
Model Peptide ◽  
Peptide System

Role of the calcium ion and the disulfide bond in the Burkholderia glumae lipase

2003 ◽  
Vol 22 (5-6) ◽  
pp. 329-338 ◽  
Author(s):  
Mohamed El Khattabi ◽  
Patrick Van Gelder ◽  
Wilbert Bitter ◽  
Jan Tommassen
Keyword(s):  
Disulfide Bond ◽  
Calcium Ion ◽  
Burkholderia Glumae

scholarly journals The role of disulfide bond isomerase A (DsbA) ofEscherichia coliO157:H7 in biofilm formation and virulence

2008 ◽  
Vol 278 (2) ◽  
pp. 213-222 ◽  
Author(s):  
Yunho Lee ◽  
Younghoon Kim ◽  
Sujin Yeom ◽  
Saehun Kim ◽  
Sungsu Park ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Biofilm Formation ◽  
Disulfide Bond Isomerase

scholarly journals Role of disulfide bond formation in the folding and assembly of the envelope glycoproteins of a pestivirus

2002 ◽  
Vol 296 (2) ◽  
pp. 470-476 ◽  
Author(s):  
Norica Branza-Nichita ◽  
Catalin Lazar ◽  
David Durantel ◽  
Raymond A Dwek ◽  
Nicole Zitzmann
Keyword(s):  
Disulfide Bond ◽  
Bond Formation ◽  
Envelope Glycoproteins ◽  
Disulfide Bond Formation

scholarly journals The Role of the Internal Disulfide Bond in the Conformational Dynamics of Neuroglobin

2010 ◽  
Vol 98 (3) ◽  
pp. 639a
Author(s):  
Luisana Astudillo ◽  
Pierre Sebban ◽  
Jaroslava Miksovska
Keyword(s):  
Disulfide Bond ◽  
Conformational Dynamics

scholarly journals A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts

2020 ◽  
Author(s):  
Charles R Midgett ◽  
Rachel A Swindell ◽  
Maria Pellegrini ◽  
F Jon Kull
Keyword(s):  
Crystal Structure ◽  
Transcription Factor ◽  
Disulfide Bond ◽  
Bile Salts ◽  
Biochemical Analysis ◽  
Conformation Analysis ◽  
Binding Partner ◽  
Bile Resistance ◽  
Periplasmic Domain

AbstractToxR is a transmembrane transcription factor that, together with its integral membrane periplasmic binding partner ToxS, is conserved across the Vibrio family. In some pathogenic Vibrios, including V. parahaemolyticus and V. cholerae, ToxR is required for bile resistance and virulence, and ToxR is fully activated and protected from degradation by ToxS. ToxS achieves this in part by ensuring formation of an intra-chain disulfide bond in the C-terminal periplasmic domain of ToxR (dbToxRp). In this study, biochemical analysis showed dbToxRp to have a higher affinity for the ToxS periplasmic domain than the non-disulfide bonded conformation. Analysis of our dbToxRp crystal structure showed this is due to disulfide bond stabilization. Furthermore, dbToxRp is structurally homologous to the V. parahaemolyticus VtrA periplasmic domain. These results highlight the critical structural role of disulfide bond in ToxR and along with VtrA define a domain fold involved in environmental sensing conserved across the Vibrio family.

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