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Several proteins have recently been found to consist of repetitive structural units in a superhelical arrangement. The structure of the leucine-rich repeat variant protein represents an unexpected addition to the list of such proteins, with the repetitive unit consisting of antiparallel α- and 310-helices.
NMR structure of an HIV-1 Rev peotide complexed with either the Rev binding elements or an RNA aptamer show that the helical peotide inserts into a widened major groove. However, significant local differences are observed.
The structure of the RuvA tetramer suggests how Holliday junctions are maintained in a conformation that facilitates branch migration during recombination.
The structure of the leucine-rich repeat variant protein reveals a novel fold consisting of alternating α- and 310-helices arranged in a right-handed superhelix that follows an N-terminal 4Fe:4S cluster-containing domain.
NMR resonances of backbone nuclei have been assigned for >95% of the residues in oxidized, substrate-free, perdeuterated 13C/15N-labelled MurB (347 residues). A novel approach utilizing minimum chemical shift changes was employed to localize the NADP+ binding site on MurB.
Buried water molecules play a pivotal structural and energetic role in mediating interactions between a bacterial oligopeptide transporter protein and its ligands.
