NDLI: Conformational analysis of putative regulatory subunit D of the toluene/o-xylene-monooxygenase complex from Pseudomonas stutzeri OX1

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Effect of the N1 residue on the stability of the α-helix for all 20 amino acids

Identification of four proteins from the small subunit of the mammalian mitochondrial ribosome using a proteomics approach.

Conformational analysis of putative regulatory subunit D of the toluene/o-xylene-monooxygenase complex from Pseudomonas stutzeri OX1

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Conformational analysis of putative regulatory subunit D of the toluene/o-xylene-monooxygenase complex from Pseudomonas stutzeri OX1

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Scognamiglio, R. Dal Piaz, F. Notomista, E. Tramontano, A. Barbieri, P. Pucci, P. Di Donato, A.
Description	Country affiliation: Italy Author Affiliation: Scognamiglio R ( Dipartimento di Chimica Organica e Biologica, Universitá di Napoli Federico II, Via Mezzocannone, 16, 80134 Naples, Italy.)
Abstract	A gene cluster isolated from Pseudomonas stutzeri OX1 genomic DNA and containing six ORFs codes for toluene/o-xylene-monooxygenase. The putative regulatory D subunit was expressed in Escherichia coli and purified. Its protein sequence was verified by mass spectrometry mapping and found to be identical to the sequence predicted on the basis of the DNA sequence. The surface topology of subunit D in solution was probed by limited proteolysis carried out under strictly controlled conditions using several proteases as proteolytic probes. The same experiments were carried out on the homologous P2 component of the multicomponent phenol hydroxylase from Pseudomonas putida CF600. The proteolytic fragments released from both proteins in their native state were analyzed by electrospray mass spectrometry, and the preferential cleavage sites were assessed. The results indicated that despite the relatively high similarity between the sequences of the two proteins, some differences in the distribution of preferential proteolytic cleavages were detected, and a much higher conformational flexibility of subunit D was inferred. Moreover, automatic modeling of subunit D was attempted, based on the known three-dimensional structure of P2. Our results indicate that, at least in this case, standard modeling procedures based on automatic alignment on the structure of P2 fail to produce a model consistent with limited proteolysis experimental data. Thus, it is our opinion that reliable techniques such as limited proteolysis can be employed to test three-dimensional models and highlight problems in automatic model building.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	10
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2001-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Models, Molecular Oxygenases Chemistry Protein Subunits Pseudomonas Enzymology Recombinant Proteins Trans-activators Amino Acid Sequence Genes, Regulator Genetics Physiology Hydrolysis Models, Chemical Metabolism Protein Conformation Research Support, Non-u.s. Gov't Validation Studies Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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