Molecular size and symmetry of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. An X-ray crystallography analysis.

Marcq, S.; Diaz-Ruano, A.; Charlier, Paulette; Dideberg, O.; Tricot, C.; Stalon, V.; Piérard, A.

doi:10.1016/0022-2836(91)90375-G

Article (Scientific journals)

Molecular size and symmetry of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. An X-ray crystallography analysis.

Marcq, S.; Diaz-Ruano, A.; Charlier, Paulette et al.

1991 • In Journal of Molecular Biology, 220 (1), p. 9-12

Peer Reviewed verified by ORBi

Permalink
https://hdl.handle.net/2268/78219

DOI
10.1016/0022-2836(91)90375-G

PubMed
1906110

Files (1)Send to Details Statistics Bibliography Similar publications

Files

Full Text

Marcq_JMB_1991.pdf

Publisher postprint (560.93 kB)

Download

All documents in ORBi are protected by a user license.

Send to

RIS BibTex APA Chicago Permalink X Linkedin

Details

Keywords :

Macromolecular Substances; Models, Structural; Ornithine Carbamoyltransferase/chemistry/isolation & purification; Protein Conformation; Pseudomonas aeruginosa/enzymology; X-Ray Diffraction/methods

Abstract :

[en] The catabolic ornithine carbamoyltransferase (EC 2.1.3.3) from Pseudomonas aeruginosa, that shows allosteric behaviour, and a mutant version of this enzyme has been crystallized in several different crystal forms. All of these have been characterized by X-ray diffraction methods. A 4.5 A resolution data set has been collected on a triclinic crystal. Analysis of the data using the self-rotation function shows that 12 monomers associate to form a particle with cubic 23 point group symmetry.

Disciplines :

Production, distribution & supply chain management

Author, co-author :

Marcq, S.

Diaz-Ruano, A.

Charlier, Paulette ; Université de Liège - ULiège > Département des sciences de la vie > Cristallographie des macromolécules biologiques

Dideberg, O.

Tricot, C.

Stalon, V.

Piérard, A.

Language :

English

Title :

Molecular size and symmetry of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. An X-ray crystallography analysis.

Publication date :

1991

Journal title :

Journal of Molecular Biology

ISSN :

0022-2836

eISSN :

1089-8638

Publisher :

Academic Press, London, United Kingdom

Volume :

220

Issue :

Pages :

9-12

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 30 November 2010

Statistics

Number of views

91 (1 by ULiège)

Number of downloads

135 (0 by ULiège)

More statistics

Scopus citations^®

Scopus citations^®
without self-citations

OpenCitations

OpenAlex citations

Bibliography

Baur, Stalon, Falmagne, Luethi, Haas (1987) Primary and quaternary structure of the catabolic OTCase from Pseudomonas aeruginosa. Extensive sequence homology with anabolic OTCase of Escherichia coli. Eur. J. Biochem 166:111-117.
Colman, Matthews (1971) Symmetry, molecular weight and crystallographic data for sweet potato β-amylase. J. Mol. Biol 60:163-168.
Fitzgerald (1988) MERLOT an integrated package of computer programs for the determination of crystal structures by molecular replacement. Journal of Applied Crystallography 21:273-278.
Haas, Evans, Mercenier, Simon, Stalon (1979) Genetic and physiological characterisation of Pseudomonas aeruginosa mutants affected in the catabolic ornithine carbamoyltransferase. J. Bacteriol 139:713-720.
Haas, Baur, Tricot, Gallimand, Stalon Recent Advances in Microbial Ecology , I. Hattori, Y. Ishida, Y. Maruyama, R.Y. Morita, A. Kochida, Japan Scientific Societies Press, Tokyo; 1989, 617-621.
Itoh, Soldati, Stalon, Falmagne, Terawaki, Leisinger, Haas (1988) Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa: nucleotide sequence and transcriptional control of the argF structural gene. J. Bacteriol 170:2725-2734.
Kuo, Seaton (1989) X-ray diffraction analysis on single crystals of recombinant Escherichia coli ornithine transcarbamoylase. J. Biol. Chem 264:16246-16248.
Matthews (1968) Solvent content of protein crystals. J. Mol. Biol 33:491-497.
Monod, Wyman, Changeux (1965) On the nature of allosteric transitions. J. Mol. Biol 12:88-108.
Ohlendorf, Lipscomb, Weber (1988) Structure and assembly of protocatechuate 3,4-dioxygenase. Nature (London) 336:403-405.
Rossmann, Brow (1962) The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallographica 15:24-31.
Satyshur, Rao, Lipscomb, Wood (1980) Preliminary crystallographic study of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. J. Biol. Chem 255:10015-10016.
Stalon, Mercenier (1984) l-Arginine utilisation by Pseudomonas species. J. Gen. Microbiol 130:69-76.
Stalon, Ramos, Piérard, Wiame (1967) Regulation of the catabolic ornithine carbamoyltransferase of Pseudomonas fluorescens. A comparison with the anabolic transferase and with a mutationally modified catabolic transferase. Biochim. Biophys. Acta 139:91-97.
Stalon, Legrain, Wiame (1977) Anabolic ornithine carbamoyltransferase of Pseudomonas. The bases of its functional specialisation. Eur. J. Biochem 74:319-327.
Vander Wauven, Piérard, Klein-Raymann, Haas (1984) Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine evidence for four gene cluster encoding the arginine deiminase pathway. J Bacteriol 160:928-934.