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The crystal structure of an iron uptake protein from pathogenic bacteria reveals elements of both divergence and convergence when compared with corresponding proteins from animals.
Combinatorial exploration of sequence space suggests five, but not three, kinds of amino acids can yield a foldable protein. Energy landscape ideas explain why such complexity might be needed.
A new phase of exploitation of neutrons has arisen from the synergy between synchrotron X-ray and neutron technique developments. The use of a much broader spectrum from reactor neutron sources than hitherto, and a very large area image plate detector sensitive to neutrons, has been applied to study the protons of lysozyme.
The time course of folding of a small β-sheet protein reveals formation of a central ligand binding cavity before the consolidation of the native hydrogen bonding network. These results suggest that side chain interactions and not stable hydrogen bonding determine the β-sheet architecture and play crucial roles in the overall chain topology.
The crystal structure at 1.8 Å resolution of 8-HDF type photolyase from A. nidulans shows a backbone structure similar to that of MTHF type E. coli photolyase but reveals a completely different binding site for the light-harvesting cofactor.
The solution NMR structure of the RNA-binding domain from influenza virus non-structural protein 1 exhibits a novel dimeric six-helical protein fold. Distributions of basic residues and conserved salt bridges of dimeric NS1(1-73) suggest that the face containing antiparallel helices 2 and 2′ forms a novel arginine-rich nucleic acid binding motif.
The nonstructural protein (NS1 protein) of the influenza A virus binds to several types of RNAs. X-ray crystallographic analysis of the RNA-binding domain reveals a unique topology for the monomer as well as a novel six-helix structure for the dimer.
The crystal structure of human replication and transcription cofactor PC4CTD reveals a dimer with two single-stranded (ss)DNA binding channels running in opposite directions to each other. This arrangement suggests a role in establishment or maintenance of melted DMA at promoters or origins of replication.
The structure of estrogen sulphotransferase has been solved in the presence of inactive cofactor PAP and substrate 17β-estradiol. This structure reveals structural similarities between cytosolic sulphotransf erases and nucleotide kinases.
