Journal ArticleDOI
Solution structure of phenol hydroxylase protein component p2 determined by nmr spectroscopy
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TLDR
The three-dimensional solution structure of P2 has been solved by 3D heteronuclear NMR spectroscopy and is the first structure among the known multicomponent oxygenases to have a conserved structure in the core regions.Abstract:
Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of binuclear iron-center-containing multicomponent oxygenases, which catalyzes the conversion of phenol and some of its methyl-substituted derivatives to catechol. In addition to a reductase component which transfers electrons from NADH, optimal turnover of the hydroxylase requires P2, a protein containing 90 amino acids which is readily resolved from the other components. The three-dimensional solution structure of P2 has been solved by 3D heteronuclear NMR spectroscopy. On the basis of 1206 experimental constraints, including 1060 distance constraints obtained from NOEs, 70 phi dihedral angle constraints, 42 psi dihedral angle constraints, and 34 hydrogen bond constraints, a total of 12 converged structures were obtained. The atomic root mean square deviation for the 12 converged structure with respect to the mean coordinates is 2.48 A for the backbone atoms and 3.85 A for all the heavy atoms. This relatively large uncertainty can be ascribed to conformational flexibility and exchange. The molecular structure of P2 is composed of three helices, six antiparallel beta-strands, one beta-hairpin, and some less ordered regions. This is the first structure among the known multicomponent oxygenases. On the basis of the three-dimensional structure of P2, sequence comparisons with similar proteins from other multicomponent oxygenases suggested that all of these proteins may have a conserved structure in the core regions.read more
Citations
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Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins
Maarten Merkx,Daniel A. Kopp,Matthew H. Sazinsky,Jessica L. Blazyk,Jens Müller,Stephen J. Lippard +5 more
TL;DR: Different aspects of catalysis by the MMO proteins are examined, including the mechanisms of dioxygen activation at the diiron site and substrate hydroxylation by the activated oxygen species.
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Biodegradation of Aromatic Compounds by Escherichia coli
TL;DR: The recent progress in the understanding of the fundamentals that govern the degradation of aromatic compounds in E. coli makes this bacterium a very useful model system to decipher biochemical, genetic, evolutionary, and ecological aspects of the catabolism of such compounds.
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Evolution of the soluble diiron monooxygenases
TL;DR: The cumulative results of phylogenetic reconstructions suggest that the alkene/aromatic Monooxygenases diverged first from the last common ancestor for these enzymes, followed by the phenol hydroxylases, Amo alkene monooxygenase, and methane mono oxygengenases.
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Metabolic reconstruction of aromatic compounds degradation from the genome of the amazing pollutant-degrading bacterium Cupriavidus necator JMP134
TL;DR: The metabolic reconstruction of aromatics degradation is performed, linking the catabolic abilities predicted in silico from the complete genome sequence with the range of compounds that support growth of this bacterium.
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Catabolism of Phenylacetic Acid in Escherichia coli CHARACTERIZATION OF A NEW AEROBIC HYBRID PATHWAY
Abel Ferrández,Baltasar Miñambres,Belén García,Elías R. Olivera,José M. Luengo,José Luis García,Eduardo Díaz +6 more
TL;DR: The paa cluster of Escherichia coli W involved in the aerobic catabolism of phenylacetic acid (PA) has been cloned and sequenced and represents a novel hybrid pathway that could be a widespread way of PACatabolism in bacteria.
References
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Journal ArticleDOI
PROCHECK: a program to check the stereochemical quality of protein structures
TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
TL;DR: The MOLSCRIPT program as discussed by the authors produces plots of protein structures using several different kinds of representations, including simple wire models, ball-and-stick models, CPK models and text labels.
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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.
David S. Wishart,Brian D. Sykes +1 more
TL;DR: It is shown that by combining both 1H and 13C chemical-shift indices to produce a ‘consensus’ estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%.