Related ArticlesNMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Biomol NMR Assign. 2013 Nov 15;
Authors: Kaplan AR, Maciejewski MW, Olson R, Alexandrescu AT
Abstract
Pathogenic bacteria secrete pore-forming toxins (PFTs) to selectively defend against immune cells and to break through cellular barriers in the host. Understanding how PFTs attack cell membranes is not only essential for therapeutic intervention but for designing agents to deliver drugs to specific human cell subtypes, for example in anti-cancer or anti-viral therapies. Many toxins contain accessory domains that help recognize specific molecular epitopes on the membranes of target cells, including proteins, carbohydrates, and lipids. Here we report NMR assignments for the 94-residue 10*kDa C-terminal accessory domain of Bacillus cereus hemolysin II, HlyIIC, that has no known structural or functional homologues. The HlyIIC domain exists in a dynamic equilibrium due to cis/trans isomerization of its Gly86-Pro87 peptide bond. The cis and trans forms are about equally populated and are in slow exchange on the NMR timescale, giving rise to separate signals for approximately half of the residues in the domain. Assignments for the cis and trans forms were achieved with the aid of a P87M mutant that stabilizes the trans form, and separate sequential walks for the two forms in 3D NMR spectra of the wild-type HlyIIC. Based on backbone chemical shifts, the domain has a ?1-?2-?1-?2-?3-?4-?3-?5 order of secondary structure elements. The last strand in the trans form and in the P87M mutant is shortened near Pro87 compared to the cis form. Both cis/trans isomerization and the P87M mutation cause large chemical shift changes throughout HlyIIC, suggesting that the proline is important in stabilizing the structure of the domain. The NMR assignments pave the way for solving the structures of the multiple conformational forms of HlyIIC and establishing their mechanism of interconversion.
PMID: 24234348 [PubMed - as supplied by publisher]
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Biomol NMR Assign. 2013 May 18;
Authors: Fonner BA, Tripet BP, Lui M, Zhu H, Lei B, Copié V
Abstract
Staphylococcus aureus is an opportunistic pathogen that...
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05-21-2013 02:34 PM
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, Cα, Cβ triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the...
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Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
J Biomol NMR. 2011 Jul 31;
Authors: Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A
We present the de novo resonance assignments for the crystalline 33*kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled...
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08-02-2011 11:40 AM
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.
Biomol NMR Assign. 2010 Dec 10;
Authors: Parnham S, Gaines WA, Duggan BM, Marcotte WR, Hennig M
The building blocks of spider dragline silk are two fibrous proteins secreted from the major ampullate gland named spidroins 1 and 2 (MaSp1, MaSp2). These proteins consist of a large central domain composed of approximately 100 tandem copies of a 35-40 amino acid repeat sequence. Non-repetitive N and...
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12-15-2010 12:03 PM
[NMR paper] NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M
NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
Related Articles NMR structures of salt-refolded forms of the 434-repressor DNA-binding domain in 6 M urea.
Biochemistry. 2004 Nov 9;43(44):13937-43
Authors: Pervushin K, Wider G, Iwai H, Wüthrich K
The N-terminal 63-residue fragment of the phage 434-repressor, 434(1-63), has a well-defined globular fold in H(2)O solution, and is unfolded in 6 M urea at pH 7.5. In this study, 434(1-63) has been refolded by adding either 1.7 M NaCl or 0.47 M NaTFA to the...
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[NMR paper] NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain
NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
Related Articles NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein.
J Mol Biol. 2002 May 10;318(4):1097-115
Authors: Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Rüterjans H, Griesinger C, Fiebig KM
We have solved the solution structure of the...
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[NMR paper] Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in fold
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
Related Articles Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
J Biomol NMR. 1994 Nov;4(6):845-58
Authors: Zhang O, Kay LE, Olivier JP, Forman-Kay JD
The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter...
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[NMR paper] Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 re
Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Complete 15N and 1H NMR assignments for the amino-terminal domain of the phage 434 repressor in the urea-unfolded form.
Proc Natl Acad Sci U S A. 1992 May 15;89(10):4397-401
Authors: Neri D, Wider G, Wüthrich K
The amino-terminal domain of the phage 434 repressor consisting of residues 1-69...
NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Linear Mode
