Elvis : Aloha from Hawaii

Die einzige Show, die Elvis Presley selbst produziert hat, sollte gleich erfolgreicher werden als die Mondlandung: Über eine Milliarde Menschen sahen weltweit am 14. Januar 1973 Aloha from Hawaii, live oder zeitversetzt. Sie machten das erste per Satellit weltweit ausgestrahlte Konzert, das in 40 Ländern über die Fernsehsender ausgestrahlt wurde, zu einem riesigen Erfolg und zu Presleys großem Comeback. Das Konzert im Neal Blaisdell Center sorgte für so viel Aufsehen, dass der Bürgermeister von Honolulu den „Elvis-Presley-Day“ am 13. Januar als hawaiianischen Feiertag ausrief. Das Elvis-Presley-Denkmal, das am 26.7.2007 in Honolulu enthüllt wurde, erinnert an den legendären Auftritt

EcoCyc: fusing model organism databases with systems biology.

EcoCyc (http://EcoCyc.org) is a model organism database built on the genome sequence of Escherichia coli K-12 MG1655. Expert manual curation of the functions of individual E. coli gene products in EcoCyc has been based on information found in the experimental literature for E. coli K-12-derived strains. Updates to EcoCyc content continue to improve the comprehensive picture of E. coli biology. The utility of EcoCyc is enhanced by new tools available on the EcoCyc web site, and the development of EcoCyc as a teaching tool is increasing the impact of the knowledge collected in EcoCyc

Crystal Structures of a Novel Ferric Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus and Its Complex with NADP+

Background: Studies performed within the last decade have indicated that microbial reduction of Fe(III) to Fe(II) is a biologically significant process. The ferric reductase (FeR) from Archaeoglobus fulgidus is the first reported archaeal ferric reductase and it catalyzes the flavin-mediated reduction of ferric iron complexes using NAD(P)H as the electron donor. Based on its catalytic activity, the A. fulgidus FeR resembles the bacterial and eukaryotic assimilatory type of ferric reductases. However, the high cellular abundance of the A. fulgidus FeR (∼0.75% of the total soluble protein) suggests a catabolic role for this enzyme as the terminal electron acceptor in a ferric iron–based respiratory pathway [1]. Results: The crystal structure of recombinant A. fulgidus FeR containing a bound FMN has been solved at 1.5 Å resolution by multiple isomorphous replacement/anomalous diffraction (MIRAS) phasing methods, and the NADP+- bound complex of FeR was subsequently determined at 1.65 Å resolution. FeR consists of a dimer of two identical subunits, although only one subunit has been observed to bind the redox cofactors. Each subunit is organized around a six-stranded antiparallel β barrel that is homologous to the FMN binding protein from Desulfovibrio vulgaris. This fold has been shown to be related to a circularly permuted version of the flavin binding domain of the ferredoxin reductase superfamily. The A. fulgidus ferric reductase is further distinguished from the ferredoxin reductase superfamily by the absence of a Rossmann fold domain that is used to bind the NAD(P)H. Instead, FeR uses its single domain to provide both the flavin and the NAD(P)H binding sites. Potential binding sites for ferric iron complexes are identified near the cofactor binding sites. Conclusions: The work described here details the structures of the enzyme-FMN, enzyme-FMN-NADP+, and possibly the enzyme-FMN-iron intermediates that are present during the reaction mechanism. This structural information helps identify roles for specific residues during the reduction of ferric iron complexes by the A. fulgidus FeR