Related ArticlesSolution conformation of cytochrome c-551 from Pseudomonas stutzeri ZoBell determined by NMR.
Biophys J. 1994 Sep;67(3):1207-15
Authors: Cai M, Timkovich R
1H NMR spectroscopy and solution structure computations have been used to examine ferrocytochrome c-551 from Pseudomonas stutzeri ZoBell (ATCC 14405). Resonance assignments are proposed for all main-chain and most side-chain protons. Stereospecific assignments were also made for some of the beta-methylene protons and valine methyl protons. Distance constraints were determined based upon nuclear Overhauser enhancements between pairs of protons. Dihedral angle constraints were determined from estimates of scalar coupling constants and intra-residue NOEs. Twenty structures were calculated by distance geometry and refined by energy minimization and simulated annealing on the basis of 1012 interproton distance and 74 torsion angle constraints. Both the main-chain and side-chain atoms are well defined except for two terminal residues, and some side-chain atoms located on the molecular surface. The average root mean squared deviation in the position for equivalent atoms between the 20 individual structures and the mean structure obtained by averaging their coordinates is 0.56 +/- 0.10 A for the main-chain atoms, and 0.95 +/- 0.09 A for all nonhydrogen atoms of residue 3 to 80 plus the heme group. The average structure was compared with an analogous protein, cytochrome c-551 from pseudomonas stutzeri. The main-chain folding patterns are very consistent, but there are some differences, some of which can be attributed to the loss of normally conserved aromatic residues in the ZoBell c-551.
[NMR paper] Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by
Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase.
Related Articles Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase.
Biochemistry. 2004 Mar 23;43(11):3167-82
Authors: Perry A, Tambyrajah W, Grossmann JG, Lian LY, Scrutton NS
Here we provide insights into the molecular structure of the two-iron...
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[NMR paper] What is the average conformation of bacteriophage T4 lysozyme in solution? A domain o
What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.
Related Articles What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.
J Mol Biol. 2001 May 11;308(4):745-64
Authors: Goto NK, Skrynnikov NR, Dahlquist FW, Kay LE
Lysozyme from T4 bacteriophage is comprised of two domains that are both involved in binding substrate. Although wild-type lysozyme has...
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[NMR paper] 1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri
1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.
Related Articles 1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.
Biochemistry. 1999 Aug 24;38(34):11164-71
Authors: Holz RC, Alvarez ML, Zumft WG, Dooley DM
1H NMR spectra of the CuA center of N2OR from Pseudomonas stutzeri, and a mutant enzyme that contains only CuA, were recorded in both H2O- and D2O-buffered solution at pH 7.5. Several sharp, well-resolved hyperfine-shifted 1H NMR signals were observed in the 60 to...
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[NMR paper] The NMR solution conformation of unligated human cyclophilin A.
The NMR solution conformation of unligated human cyclophilin A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution conformation of unligated human cyclophilin A.
J Mol Biol. 1997 Sep 12;272(1):64-81
Authors: Ottiger M, Zerbe O, Güntert P, Wüthrich K
The nuclear magnetic resonance (NMR) solution structure of free, unligated cyclophilin A (CypA), which is an 18 kDa protein from human T-lymphocytes that was expressed in Escherichia coli for the present...
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[NMR paper] Sequential 1H, 13C, and 15N NMR assignments and solution conformation of apokedarcidi
Sequential 1H, 13C, and 15N NMR assignments and solution conformation of apokedarcidin.
Related Articles Sequential 1H, 13C, and 15N NMR assignments and solution conformation of apokedarcidin.
Biochemistry. 1994 Sep 27;33(38):11438-52
Authors: Constantine KL, Colson KL, Wittekind M, Friedrichs MS, Zein N, Tuttle J, Langley DR, Leet JE, Schroeder DR, Lam KS
Kedarcidin is a recently discovered antitumor antibiotic chromoprotein. The solution conformation of the kedarcidin apoprotein (114 residues) has been characterized by heteronuclear...
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[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
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[NMR paper] Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determine
Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Related Articles Solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa as determined by two-dimensional 1H NMR.
Biochemistry. 1991 Sep 17;30(37):9040-6
Authors: Detlefsen DJ, Thanabal V, Pecoraro VL, Wagner G
The solution structure of Fe(II) cytochrome c551 from Pseudomonas aeruginosa based on 2D 1H NMR data is reported. Two sets of structure calculations were completed with a combination of simulated annealing...
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[NMR paper] 15N NMR spectroscopy of Pseudomonas cytochrome c-551.
15N NMR spectroscopy of Pseudomonas cytochrome c-551.
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Biochemistry. 1990 Aug 21;29(33):7773-80
Authors: Timkovich R
15N-1H correlation spectroscopy with detection at the 1H frequency has been used at natural abundance to detect nitrogen nuclei bonded to protons in the ferrocytochrome c-551 from Pseudomonas aeruginosa (ATCC 19429). Side-chain aromatic nitrogens, main-chain amides, and side-chain amides have been assigned to specific residues by comparison to previous proton...