Related ArticlesNMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
J Biol Chem. 2004 Jul 23;279(30):31599-605
Authors: Xu XF, Tan YW, Lam L, Hackett J, Zhang M, Mok YK
The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with known structure, t-PilS contains many distinct structural features. The protein contains an extra pair of beta-strands in the N-terminal alphabeta loop that align with the major beta-strands to form a continuous 7-stranded antiparallel beta-sheet. The C-terminal disulfide-bonded region of t-PilS is only half the length of that of toxin-coregulated pilus pilin. A model of S. typhi pilus has been proposed and mutagenesis studies suggested that residues on both the alphabeta loop and the C-terminal disulfide-bonded region of PilS might be involved in binding specificity of the pilus. This model structure reveals an exposed surface between adjacent subunits of PilS that could be a potential binding site for the cystic fibrosis transmembrane conductance regulator.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
...
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[NMR paper] Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredox
Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.
Related Articles Crystal structure and solution NMR dynamics of a D (type II) peroxiredoxin glutaredoxin and thioredoxin dependent: a new insight into the peroxiredoxin oligomerism.
Biochemistry. 2005 Feb 15;44(6):1755-67
Authors: Echalier A, Trivelli X, Corbier C, Rouhier N, Walker O, Tsan P, Jacquot JP, Aubry A, Krimm I, Lancelin JM
Peroxiredoxins (Prxs) constitute a family of...
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[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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[NMR paper] NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly
NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
Related Articles NMR structure of bacterial ribosomal protein l20: implications for ribosome assembly and translational control.
J Mol Biol. 2002 Oct 11;323(1):143-51
Authors: Raibaud S, Lebars I, Guillier M, Chiaruttini C, Bontems F, Rak A, Garber M, Allemand F, Springer M, Dardel F
L20 is a specific protein of the bacterial ribosome, which is involved in the early assembly steps of the 50S subunit and in the feedback control of the...
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[NMR paper] Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Pilin C-terminal peptide binds asialo-GM1 in liposomes: a 2H-NMR study.
Protein Sci. 1997 Nov;6(11):2459-61
Authors: Jones DH, Hodges RS, Barber KR, Grant CW
Wideline 2H-NMR observations are...
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[NMR paper] Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin
Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure and dynamics of a protein assembly. 1H-NMR studies of the 36 kDa R6 insulin hexamer.
J Mol Biol. 1996 Apr 26;258(1):136-57
Authors: Jacoby E, Hua QX, Stern AS, Frank BH, Weiss MA
The structure and dynamics of the R6 human insulin hexamer are investigated by two- and three-dimensional homonuclear 1H-NMR spectroscopy....
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[NMR paper] NMR characterization of side chain flexibility and backbone structure in the type I a
NMR characterization of side chain flexibility and backbone structure in the type I antifreeze protein at near freezing temperatures.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR characterization of side chain flexibility and backbone structure in the type I antifreeze protein at near freezing temperatures.
Biochemistry. 1996 Dec 24;35(51):16698-704
Authors: Gronwald W, Chao H, Reddy DV, Davies PL, Sykes BD, Sönnichsen FD
The flexibility of the polar side chains in the...
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[NMR paper] Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR.
Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nsb.gif Related Articles Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR.
Nat Struct Biol. 1999 Apr;6(4):336-9
Authors: Pellecchia M, Sebbel P, Hermanns U, Wüthrich K, Glockshuber R
The 23 kDa two-domain periplasmic chaperone FimC from Escherichia coli is required for the assembly of type-1 pili, which are filamentous, highly oligomeric protein complexes anchored to the outer...
NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
Linear Mode
