Related ArticlesThree-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species.
Biochemistry. 1995 Aug 8;34(31):9851-8
Authors: Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P
The NMR solution structure of the oxidized HiPIP from Chromatium vinosum has been solved. Despite the fact that the protein is paramagnetic, 85% of the 1H and 80% of the 15N signals have been assigned. Through 1537 NOEs, out of which 1142 were found to be relevant for the structure determination, a family of structures has been obtained by distance geometry calculations. These structures have then been subjected to restrained energy minimization (REM) and restrained molecular dynamics (RMD) calculations in vacuum. Finally, the mean structure of the RMD family has been treated through RMD in water. The RMSD values for the backbone and heavy atoms within the RMD family are 0.57 +/- 0.14 and 1.08 +/- 0.16 A, respectively. These values together with other parameters indicate that the structure is of good quality and as good as the structure of the reduced protein. The RMDw structures of the reduced and oxidized proteins are different beyond the experimental indetermination. The set of constraints for the reduced and oxidized forms have been used to treat the available X-ray structure by RMD in water. The two structures generated in this way are quite similar to their respective solution structures, thus confirming that the experimental constraints are capable of yielding two different structures from the same starting structural model. This is the first time that independently determined solution structures of two redox states of a paramagnetic protein are available. Differences between them and the X-ray structure are discussed.
[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] Identification of slow motions in the reduced recombinant high-potential iron sulfur
Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
Related Articles Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
J Biomol NMR. 1998 Aug;12(2):307-18
Authors: Banci L, Felli IC, Koulougliotis D
Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been...
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[NMR paper] Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin
Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Related Articles Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H...
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Fully automated high-quality NMR structure determination of small (2)H-enriched prote
Fully automated high-quality NMR structure determination of small (2)H-enriched proteins.
Related Articles Fully automated high-quality NMR structure determination of small (2)H-enriched proteins.
J Struct Funct Genomics. 2010 Aug 24;
Authors: Tang Y, Schneider WM, Shen Y, Raman S, Inouye M, Baker D, Roth MJ, Montelione GT
Determination of high-quality small protein structures by nuclear magnetic resonance (NMR) methods generally requires acquisition and analysis of an extensive set of structural constraints. The process generally demands...
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[NMR paper] 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhod
1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans.
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 1H NMR of high-potential iron-sulfur protein from the purple non-sulfurbacterium Rhodoferax fermentans.
Eur J Biochem. 1996 Mar 1;236(2):405-11
Authors: Ciurli S, Cremonini MA, Kofod P, Luchinat C
Oxidized and reduced forms of high-potential iron-sulfur protein (HiPIP) from the...
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[NMR paper] The three-dimensional solution structure of the reduced high-potential iron-sulfur pr
The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Related Articles The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
Biochemistry. 1995 Jan 10;34(1):206-19
Authors: Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P
The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature has been extended up to 85% of the total protein protons. Ninety...
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[NMR paper] 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from
1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.
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 1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.
Eur J Biochem. 1993 Feb 15;212(1):69-78
Authors: Bertini I, Capozzi F, Luchinat C, Piccioli M
1H one-dimensional and two-dimensional NMR spectra have been...
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[NMR paper] 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nucle
1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
Related Articles 1H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements.
Biochemistry. 1990 Jun 12;29(23):5633-7
Authors: Cowan JA, Sola M
1H nuclear Overhauser effect experiments on the isotropically shifted signals of oxidized Chromatium vinosum HiPIP have been used to identify the four beta-CH2 geminal couples of the cysteine ligands. A partial assignment to...
Three-dimensional solution structure of the oxidized high potential iron-sulfur prote
Linear Mode
