| Literature DB >> 16797012 |
Valentina Buttani1, Aba Losi, Eugenia Polverini, Wolfgang Gärtner.
Abstract
The blue-light sensitive protein YtvA from Bacillus subtilis is built of a photoactive, flavin-binding LOV (Light, Oxygen and Voltage) domain and a STAS domain with unknown function. Here we show that YtvA binds a fluorescent derivative of guanosine triphosphate (GTPTR) that can be displaced by both GTP or ATP. Unspecific NTP (N=G or A) binding is supported by the molecular model of YtvA-STAS. Blue-light activation of YtvA results in small and dark-reversible spectroscopic changes for GTPTR, suggesting that light-driven conformational changes are transmitted from the LOV core to the GTPTR binding site. These results support the idea that STAS domains may have a general NTP binding role and open a way to investigate the molecular functionality of YtvA-STAS.Entities:
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Year: 2006 PMID： 16797012 DOI： 10.1016/j.febslet.2006.06.007
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124