Pregled bibliografske jedinice broj: 123858
Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis
Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis // Biochimie, 86 (2004), 6; 403-409 doi:10.1016/j.biochi.2004.05.001 (međunarodna recenzija, članak, znanstveni)
CROSBI ID: 123858 Za ispravke kontaktirajte CROSBI podršku putem web obrasca
Naslov
Metal-ion induced conformational changes in
alkaline phosphatase from E. coli assessed by
limited proteolysis
Autori
Bučević-Popović, Viljemka ; Pavela-Vrančič, Maja ; Dieckmann, Ralf
Izvornik
Biochimie (0300-9084) 86
(2004), 6;
403-409
Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni
Ključne riječi
Alkaline phosphatase ; metal ion ; conformational change ; limited proteolysis ; MALDI-TOF mass spectrometry
Sažetak
Alkaline phosphatase (AP) displays significant structural changes during metal-ion binding, supporting cooperative interactions between the subunits of the dimeric enzyme. Here, we present data on the dynamic properties of AP from E. coli, and characterize the structural changes that accompany variations in metal-ion content, combining limited proteolysis and MALDI-TOF mass spectrometry. Limited proteolysis revealed an internal cleavage site at Arg-293, reflecting a position of conformational flexibility supporting subunit communication essential for catalysis. A specific shielding of a region distant from the metal-binding site has been demonstrated, implying transmission of conformational changes, induced by metal-ion binding to the adjacent subunit, across the subunit interface.
Izvorni jezik
Engleski
Znanstvena područja
Kemija, Biologija
Citiraj ovu publikaciju:
Časopis indeksira:
- Current Contents Connect (CCC)
- Web of Science Core Collection (WoSCC)
- Science Citation Index Expanded (SCI-EXP)
- SCI-EXP, SSCI i/ili A&HCI
- Scopus
- MEDLINE
