Related ArticlesHigh-resolution solution NMR structure of the Z domain of staphylococcal protein A.
J Mol Biol. 1997 Oct 3;272(4):573-90
Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are targets for protein engineering efforts and for the development of computational approaches for de novo protein folding. The NMR solution structure of an engineered IgG-binding domain of SpA, the Z domain (an analog of the B domain of SpA), has been determined by simulated annealing with restrained molecular dynamics on the basis of 671 conformational constraints. The Z domain contains three well-defined alpha-helices corresponding to polypeptide segments Lys7 to Leu17 (helix 1), Glu24 to Asp36 (helix 2), and Ser41 to Ala54 (helix 3). A family of ten conformers representing the solution structure of the Z domain was computed by simulated annealing of restrained molecular dynamics using the program CONGEN. The average of the root-mean-square deviations (r.m. s.d.) of the individual NMR conformers, relative to the mean coordinates, for the backbone atoms N, Calpha and C' of residues Phe5 through Ala56 is 0.69 A; the corresponding backbone r.m.s.d. for the three-helical core is 0.44 A. Helices 1, 2 and 3 are antiparallel in orientation (Omega12=-170(+/-4) degrees , Omega13=+16(+/-3) degrees , Omega23=+173(+/-7) degrees ). A comparison of backbone amide hydrogen/deuterium exchange rates in free and IgG-bound Z domains demonstrates that the amide protons of helices 1, 2 and 3 are protected from rapid exchange in both states, indicating that all three helices are also intact in the IgG-bound state. These solution NMR results differ from the previously determined X-ray structure of the similar SpA B domain in complex with the Fc fragment of a human IgG antibody, where helix 3 is not observed in the electron density map and from the solution NMR structure of the B domain, where helix 3 is observed but helix 1 is tilted by approximately 30 degrees with respect to helices 2 and 3. Hydrogen-bonded N-cap and C-cap formation is observed for all three helices of the Z domain; these capping interactions appear to be highly conserved in the five homologous domains of SpA.
[NMR paper] High-resolution solution NMR structure of the minimal active domain of the human immu
High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Related Articles High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Biochemistry. 1998 Dec 22;37(51):17704-13
Authors: Kodera Y, Sato K, Tsukahara T, Komatsu H, Maeda T, Kohno T
The retroviral nucleocapsid (NC) protein is a multifunctional protein essential for RNA genome packaging and viral infectivity. The NC protein, NCp8, of the...
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[NMR paper] High-resolution solution structure of the inhibitor-free catalytic fragment of human
High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
Related Articles High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
Biochemistry. 1998 Feb 10;37(6):1495-504
Authors: Moy FJ, Chanda PK, Cosmi S, Pisano MR, Urbano C, Wilhelm J, Powers R
The high-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase (MMP-1), a...
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[NMR paper] High resolution NMR solution structure of the leucine zipper domain of the c-Jun homo
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
J Biol Chem. 1996 Jun 7;271(23):13663-7
Authors: Junius FK, O'Donoghue SI, Nilges M, Weiss AS, King GF
The solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new...
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[NMR paper] Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectr
Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy.
Biochemistry. 1996 Mar 5;35(9):2845-53
Authors: Jaishree TN, Ramakrishnan V, White SW
The solution of a primary 16S rRNA-binding ribosomal protein, S17, was investigated by two- and three-dimensional homonuclear and heteronuclear magnetic resonance...
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[NMR paper] Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR
Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Related Articles Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Biochemistry. 1994 May 31;33(21):6408-17
Authors: Qi PX, Di Stefano DL, Wand AJ
A model for the solution structure of horse heart ferrocytochrome c has been determined by nuclear magnetic resonance spectroscopy combined with hybrid distance geometry-simulated annealing calculations....
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[NMR paper] Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR
Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Related Articles Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Biochemistry. 1994 May 31;33(21):6408-17
Authors: Qi PX, Di Stefano DL, Wand AJ
A model for the solution structure of horse heart ferrocytochrome c has been determined by nuclear magnetic resonance spectroscopy combined with hybrid distance geometry-simulated annealing calculations....
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[NMR paper] High-resolution structure of the oligomerization domain of p53 by multidimensional NM
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Related Articles High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science. 1994 Jul 15;265(5170):386-91
Authors: Clore GM, Omichinski JG, Sakaguchi K, Zambrano N, Sakamoto H, Appella E, Gronenborn AM
The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a...
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[NMR paper] High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distan
High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach.
Related Articles High-resolution structure of an HIV zinc fingerlike domain via a new NMR-based distance geometry approach.
Biochemistry. 1990 Jan 16;29(2):329-40
Authors: Summers MF, South TL, Kim B, Hare DR
A new method is described for determining molecular structures from NMR data. The approach utilizes 2D NOESY back-calculations to generate simulated spectra for structures obtained from distance geometry (DG) computations. Comparison...