Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/13456
Title: NMR structural studies on the pilin monomer pils from Salmonella typhi
Authors: XU XINGFU
Keywords: Type IVb pilin, NMR, adhesin, assignment, solution structure
Issue Date: 6-Jan-2004
Source: XU XINGFU (2004-01-06). NMR structural studies on the pilin monomer pils from Salmonella typhi. ScholarBank@NUS Repository.
Abstract: PilS is a type IVb pilin that assembles to form the pili of Salmonella typhi. The pilus is believed to be a major adhesin for the entry of this pathogen into intestinal epithelial cells via binding to CFTR. N-terminal truncated form of PilS was expressed, purified and studied by NMR. Near complete backbone and side chain resonance assignments were obtained using 15N and 13C labeled sample. Protein structure determined using NOE, hydrogen bond and dihedral angle restraints suggested that PilS adopted an I?/I? pilin fold containing 4 I?-helices packed against an anti-parallel I?-sheet formed by 7 I?-strands. The solution structure of pils is similar to the recently determined crystal structure of TCP pilin but with substantial differences.
URI: http://scholarbank.nus.edu.sg/handle/10635/13456
Appears in Collections:Master's Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
XUXF_MSc.pdf3.22 MBAdobe PDF

OPEN

NoneView/Download

Page view(s)

201
checked on Dec 11, 2017

Download(s)

153
checked on Dec 11, 2017

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.