Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes

The structural and functional characterization of Isd-LmHde, an Isd-type haem-degrading enzyme in Listeria monocytogenes, is presented. The haem-degradation product of Isd-LmHde was verified to be biliverdin and the active residues were identified by structure-based mutagenesis and following function studies.

Structural insights into the molecular mechanism of Escherichia coli SdiA, a quorum-sensing receptor

Crystal structures of the full-length E. coli quorum-sensing receptor SdiA reveal that it forms a symmetrical dimer and exhibits broad ligand-binding selectivity. The ligand binding increases the stability of SdiA but does not modulate its DNA-binding ability. The DNA-binding activity of SdiA can be regulated through the formation of an intersubunit disulfide bond.

Structural and functional characterization of an Isd-type haem-degradation enzyme from Listeria monocytogenes. Corrigendum

A correction is made to the article by Duong et al. [(2014). Acta Cryst. D70, 615-626] .