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Expression, Purification, Structural and Functional Analysis of SycB: A Type Three Secretion Chaperone From Yersinia Enterocolitica

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Title Expression, Purification, Structural and Functional Analysis
of SycB: A Type Three Secretion Chaperone From Yersinia
Enterocolitica
 
Creator Basu, Abhishek
Chatterjee, Rakesh
Datta, Saumen
 
Subject Structural Biology & Bioinformatics
 
Description In Yersinia enterocolitica biovar 1B, a genome
encoded TTSS designated as Ysa-Ysp system is used for
virulence. SycB is an annotated chaperone to this system.
SycB is soluble in presence of translocator YspC. SycB and
its truncated form (DSycB(1–114)) exist as dimers. YspC
forms a 1:1 complex with SycB. Homology model of SycB
shows a flexible N-terminal may be required for solubility
and dimerization; and concave core formed by antiparallel
helices of TPRs. Far UV CD spectra confirm that SycB is
predominantly alpha helical. Near UV CD spectra show that
SycB has tertiary structure at pH 7.2 (native folded protein),
which disappears at pH 5 (molten globule) and SycB
releases YspC at pH 5. SycB has a cooperative melting
behavior. At pH 7.2, SycB shows solvent accessible
hydrophobic patches. Concave core in the model exhibits
ANS binding within FRET distance of tyrosines in the TPR,
allowing a range of interaction of SycB with its ligand.
 
Publisher Kluwer
 
Date 2012
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/1568/1/PROTEIN_JOURNAL___31_(1)93%2D107;2012[94].pdf
Basu, Abhishek and Chatterjee, Rakesh and Datta, Saumen (2012) Expression, Purification, Structural and Functional Analysis of SycB: A Type Three Secretion Chaperone From Yersinia Enterocolitica. The Protein Journal, 31 (1). pp. 93-107.
 
Relation http://dx.doi.org/10.1007/s10930-011-9377-2
http://www.eprints.iicb.res.in/1568/