Related ArticlesPilus 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 bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces. Here we identified the contact sites on the surface of the NMR structure of FimC that are responsible for the binding of the 28 kDa mannose-binding type-1 pilus subunit FimH by 15N and 1H NMR chemical shift mapping, using transverse relaxation-optimized spectroscopy (TROSY). The FimH-binding surface of FimC is formed nearly entirely by the N-terminal domain, and its extent and shape indicate that FimC binds a folded form of the pilus subunits.
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein.
FEBS J. 2005 Feb;272(3):865-71
Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A
The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...
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11-24-2010 11:14 PM
[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Biochemistry. 2004 Nov 2;43(43):13775-86
Authors: Bann JG, Frieden C
The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...
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[NMR paper] NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.
Related Articles NMR 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...
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11-24-2010 09:51 PM
[NMR paper] 3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR expe
3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR experiments with two sequential connectivity pathways and high sensitivity.
Related Articles 3D TROSY-HNCA(coded)CB and TROSY-HNCA(coded)CO experiments: triple resonance NMR experiments with two sequential connectivity pathways and high sensitivity.
J Biomol NMR. 2004 Mar;28(3):289-94
Authors: Ritter C, Lührs T, Kwiatkowski W, Riek R
The concept of chemical shift-coding monitors chemical shifts in multi-dimensional NMR experiments without additional polarization...
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11-24-2010 09:25 PM
[NMR paper] Base flexibility in HIV-2 TAR RNA mapped by solution (15)N, (13)C NMR relaxation.
Base flexibility in HIV-2 TAR RNA mapped by solution (15)N, (13)C NMR relaxation.
Related Articles Base flexibility in HIV-2 TAR RNA mapped by solution (15)N, (13)C NMR relaxation.
J Mol Biol. 2002 Mar 22;317(2):263-78
Authors: Dayie KT, Brodsky AS, Williamson JR
Binding of the HIV tat protein to the TAR (transactivating response region) RNA element activates transcription of the HIV viral genome. The complex of TAR with argininamide serves as a model for the RNA conformation in the tat-TAR complex. The dynamics of the HIV-2 TAR-argininamide...
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11-24-2010 08:49 PM
[NMR paper] NMR structure and metal interactions of the CopZ copper chaperone.
NMR structure and metal interactions of the CopZ copper chaperone.
Related Articles NMR structure and metal interactions of the CopZ copper chaperone.
J Biol Chem. 1999 Aug 6;274(32):22597-603
Authors: Wimmer R, Herrmann T, Solioz M, Wüthrich K
A recently discovered family of proteins that function as copper chaperones route copper to proteins that either require it for their function or are involved in its transport. In Enterococcus hirae the copper chaperone function is performed by the 8-kDa protein CopZ. This paper describes the NMR...
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11-18-2010 08:31 PM
[NMR paper] NMR solution structure of the periplasmic chaperone FimC.
NMR solution structure of the periplasmic chaperone FimC.
Related Articles NMR solution structure of the periplasmic chaperone FimC.
Nat Struct Biol. 1998 Oct;5(10):885-90
Authors: Pellecchia M, Güntert P, Glockshuber R, Wüthrich K
The NMR structure of the 205-residue periplasmic chaperone FimC is presented. This protein consists of two globular domains with immunoglobulin-like folds connected by a 15-residue linker peptide. The relative orientation of the two domains is defined by hydrophobic contacts and an interdomain salt bridge. FimC...
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11-17-2010 11:15 PM
[NMR paper] TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagne
TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.
Related Articles TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.
Biochemistry. 1998 Jul 7;37(27):9650-7
Authors: Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR
Surfaces of the 173 residue catalytic domain of human matrix metalloproteinase 3 (MMP-3(DeltaC)) affected by binding of the N-terminal, 126 residue inhibitory domain of human TIMP-1...
Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR.
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