Articles in 2012

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  • Biotechnological applications of hydrogenases are limited by their susceptibility to inactivation by oxygen, thought to proceed by trapping a reduced O2 in the active site. Electrochemical and spectroscopic studies using various electron acceptors now show that oxygen inactivation is not linked to oxygen atom donation.

    • Abbas Abou Hamdan
    • Bénédicte Burlat
    • Sébastien Dementin
    Brief Communication
  • Acanthaporin is identified as a pore-forming protein from the infectious Acanthamoeba culbertsoni with a previously unknown structure. The newly identified structure includes a pH-dependent histidine switch that controls partitioning between the inactive dimer and the active monomer, which assembles into larger species to cause toxicity.

    • Matthias Michalek
    • Frank D Sönnichsen
    • Matthias Leippe
    Article
  • Src family kinase mutants, with altered regulatory domain interactions, were profiled with a photodependent crosslinking strategy to reveal conformation-specific ATP-competitive inhibitors that affect intermolecular binding interactions.

    • Ratika Krishnamurty
    • Jennifer L Brigham
    • Dustin J Maly
    Article
  • Post-translational modification of proteins by N-acetylglucosamine (O-GlcNAc) is carried out by a single glycosyltransferase, OGT. Two independent groups have generated structures of ternary complexes that elegantly illuminate substrate and product binding modes, and thus the overall reaction coordinate, but the respective authors differ in their choice of catalytic base.

    • Stephen G Withers
    • Gideon J Davies
    News & Views
  • Understanding the reaction mechanism of OGT, responsible for O-GlcNAcylating various protein substrates, has been hampered by a lack of structural information. Snapshots of ternary complexes along the reaction coordinate now provide evidence for substrate participation in an electrophilic migration mechanism.

    • Michael B Lazarus
    • Jiaoyang Jiang
    • Suzanne Walker
    Brief Communication
  • Riboswitches—RNA motifs that regulate gene expression in response to binding of specific ligands—have been identified for many small-molecule metabolites. An ATP-binding element in the ydaO mRNA of Bacillus subtilis provides the first example of an ATP-responsive riboswitch.

    • Peter Y Watson
    • Martha J Fedor
    Brief Communication