Crystallization, X-ray Diffraction Analysis and Phasing of 17beta-Hydroxysteroid Dehydrogenase from fungus Cochliobolus lunatus (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Crystallization, X-ray Diffraction Analysis and Phasing of 17beta-Hydroxysteroid Dehydrogenase from fungus Cochliobolus lunatus (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Cassetta A., Büdefeld T., Lanišsnik Rižner T., Kristan K., Stojan J., Lamba D. (2005)
  Crystallization, X-ray Diffraction Analysis and Phasing of 17beta-Hydroxysteroid Dehydrogenase from fungus Cochliobolus lunatus
  in Acta crystallographica. Section F
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Cassetta A., Büdefeld T., Lanišsnik Rižner T., Kristan K., Stojan J., Lamba D. (literal)

Pagina inizio

• 1032 (literal)

Pagina fine

• 1034 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 61 (literal)

Rivista

• Acta crystallographica. Section F. Structural biology and crystallization communications (Rivista)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)
• PubMe (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Büdefeld T., Lanisšnik Rižner T., Kristan K., Stojan J., Institute of Biochemistry, Medical Faculty Ljubljana, Slovenia Cassetta A. IC-CNR, Trieste Lamba D. IC-CNR, Trieste (literal)

Titolo

• Crystallization, X-ray Diffraction Analysis and Phasing of 17beta-Hydroxysteroid Dehydrogenase from fungus Cochliobolus lunatus (literal)

Abstract

• 17?-Hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus (17?-HSDcl) is an NADP(H)-dependent enzyme that preferentially catalyses the oxidoreduction of oestrogens and androgens. The enzyme belongs to the short-chain dehydrogenase/reductase superfamily and is the only fungal hydroxysteroid dehydrogenase known to date. 17?-HSDcl has recently been characterized and cloned and has been the subject of several functional studies. Although several hypotheses on the physiological role of 17?-HSDcl in fungal metabolism have been formulated, its function is still unclear. An X-ray crystallographic study has been undertaken and the optimal conditions for crystallization of 17?-HSDcl (apo form) were established, resulting in well shaped crystals that diffracted to 1.7 A resolution. The space group was identified as I4(1)22, with unit-cell parameters a = b = 67.14, c = 266.77 A. Phasing was successfully performed by Patterson search techniques. A catalytic inactive mutant Tyr167Phe was also engineered, expressed, purified and crystallized for functional and structural studies. (literal)

Prodotto di

• Institute of Crystallography (IC) (Istituto)
• Studi strutturali e funzionali di proteine di interesse biomedico e biotecnologico (PM.P01.023.001) (Modulo)

Autore CNR

• ALBERTO CASSETTA (Persona)
• DORIANO LAMBA (Unità di personale interno)

Incoming links:

Prodotto

• Institute of Crystallography (IC) (Istituto)
• Studi strutturali e funzionali di proteine di interesse biomedico e biotecnologico (PM.P01.023.001) (Modulo)

Autore CNR di

• ALBERTO CASSETTA (Persona)
• DORIANO LAMBA (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Acta crystallographica. Section F. Structural biology and crystallization communications (Rivista)