Related ArticlesNMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556).
J Biol Inorg Chem. 2004 Mar;9(2):224-30
Authors: Bertini I, Faraone-Mennella J, Gray HB, Luchinat C, Parigi G, Winkler JR
The structure of oxidized Rhodopseudomonas palustris cytochrome c(556) has been modeled after that of high-spin cytochrome c' from the same bacterium, the latter being the protein with the greatest sequence identity (35%) among all sequenced proteins in the genomes. The two proteins differ in the number of ligands to iron and in spin state, the former being six-coordinate low-spin and the latter five-coordinate high-spin. In order to validate this modeled structure, several structural restraints were obtained by performing a restricted set of NMR experiments, without performing a complete assignment of the protein signals. The aim was to exploit the special restraints arising from the paramagnetism of the metal ion. A total of 43 residual-dipolar-coupling and 74 pseudocontact-shift restraints, which together sampled all regions of the protein, were used in conjunction with over 40 routinely obtained NOE distance restraints. A calculation procedure was undertaken combining the program MODELLER and the solution structure determination program PARAMAGNETIC DYANA, which includes paramagnetism-based restraints. The directions and magnitude of the magnetic susceptibility anisotropy tensor were also calculated. The approach readily provides useful results, especially for paramagnetic metalloproteins of moderate to large dimensions.
[NMR paper] 1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing
1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme Moiety.
Related Articles 1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme Moiety.
Inorg Chem. 1998 Sep 21;37(19):4814-4821
Authors: Bertini I, Dikiy A, Luchinat C, Macinai R, Viezzoli MS
The assignment of the hyperfine shifted signals of the reduced cytochrome c' from Rhodopseudomonas palustris has been obtained through saturation transfer experiments with assigned signals...
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NMR structure note: oxidized microsomal human cytochrome b5.
NMR structure note: oxidized microsomal human cytochrome b5.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: oxidized microsomal human cytochrome b5.
J Biomol NMR. 2010 Aug;47(4):289-95
Authors: Nunez M, Guittet E, Pompon D, van Heijenoort C, Truan G
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[NMR paper] An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1[Fe4
An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1 ferredoxin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1 ferredoxin.
Eur J Biochem. 1996 May 1;237(3):726-35
Authors: Sticht H, Wildegger G, Bentrop D, Darimont B, Sterner R, Rösch P
The solution structure of the 60-residue 1 ferredoxin from the hyperthermophilic...
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[NMR paper] Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing su
Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion-binding studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion-binding studies.
Eur J Biochem. 1995 Oct 1;233(1):335-9
Authors: Battistuzzi G, Borsari M, Dallari D, Ferretti S, Sola M
The effects of...
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[NMR paper] Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2 pH-dependen
Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2 pH-dependent conformational states.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2 pH-dependent conformational states.
Eur J Biochem. 1995 Aug 15;232(1):206-13
Authors: Battistuzzi G, Borsari M, Ferretti S, Sola M, Soliani E
The pH-induced protein conformational transitions and...
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[NMR paper] An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-
An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Related Articles An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Biochemistry. 1994 May 31;33(21):6424-32
Authors: Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA
A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the...
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[NMR paper] An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-
An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Related Articles An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Biochemistry. 1994 May 31;33(21):6424-32
Authors: Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA
A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the...
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NMR structure note: oxidized microsomal human cytochrome b5
NMR structure note: oxidized microsomal human cytochrome b5
Content Type Journal Article
DOI 10.1007/s10858-010-9428-6
Authors
Marcela Nunez, CNRS Centre de Génétique Moléculaire Av. de la Terrasse Gif-sur-Yvette 91198 France
Eric Guittet, CNRS Institut de Chimie de Substances Naturelles av. de la Terrasse Gif-sur-Yvette 91198 France
Denis Pompon, CNRS Centre de Génétique Moléculaire Av. de la Terrasse Gif-sur-Yvette 91198 France