Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution (Articolo in rivista)

Type
Label
  • Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution (Articolo in rivista) (literal)
Anno
  • 1998-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1107/S090744499701216X (literal)
Alternative label
  • Francesca Gliubich ab, Rodolfo Berni c, Marcello Colapietro d, Luisa Barba e, Giuseppe Zanotti a (1998)
    Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution
    in Acta crystallographica. Section D, Biological crystallography.; Blackwell, Oxford (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Francesca Gliubich ab, Rodolfo Berni c, Marcello Colapietro d, Luisa Barba e, Giuseppe Zanotti a (literal)
Pagina inizio
  • 481 (literal)
Pagina fine
  • 486 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://scripts.iucr.org/cgi-bin/paper?S090744499701216X (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 54 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 6 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 4 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • a Department of Organic Chemistry, University of Padova and Biopolymer Research Center, CNR, 35131, Padova, Italy, b Institute of Pharmaceutical Chemistry, University of Milano, 20135 Milano, Italy, c Institute of Biochemical Sciences, University of Parma, 43100 Parma, Italy, d Department of Chemistry, University of Rome `La Sapienza', 00185 Roma, Italy e Centro di Strutturistica Chimica `G. Giacomello', Sezione di Trieste, 34012 Trieste, Italy. (literal)
Titolo
  • Structure of Sulfur-Substituted Rhodanese at 1.36 Å Resolution (literal)
Abstract
  • 1.36 Å resolution X-ray diffraction data have been recorded at 100 K for bovine liver sulfur-substituted rhodanese, using synchrotron radiation. The crystal structure has been refined anisotropically to a final R factor of 0.159 (Rfree = 0.229) for 53 034 unique reflections. The model contains 2 327 protein atoms and 407 solvent molecules, with a good geometry. The high resolution allows full details for helices, [beta]-sheets, tight turns and of all inter- and intramolecular interactions stabilizing the enzyme molecule to be given. The situation at the active site is described, particularly in regard to the network of hydrogen bonds made by S[gamma] and S[delta] of the sulfur-substituted catalytic Cys247 and surrounding groups and solvent molecules. The replacement of the precipitant ammonium sulfate with cryoprotectants in the crystal-suspending medium led to the removal of the sulfate ion from the enzyme active site. Only limited changes of the enzyme structure have been found as a result of the drastic change in the crystal medium. (literal)
Editore
Prodotto di
Autore CNR

Incoming links:


Autore CNR di
Prodotto
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Editore di
data.CNR.it