Correspondence

The flavin mononucleotide (FMN)-binding protein from Desulfovibrio vulgaris (Miyazaki F) is structurally related to a so far hypothetical single-domain precursor of chymotrypsin, with the FMN-binding site coinciding with part of the active site of the protease.

NMR spectroscopy has been used to determine that the dimerization interface of UmuD' in solution is not the homodimer interface originally inferred from crystallographic data. Instead, it resembles an interface that had been hypothesized to be involved in filamentation.

NMR studies of the lymphoproliferation mutant (V238N) of the Fas death domain indicate that helix 3 is unfolded. This local structural change abolishes binding to FADD — a protein that interacts with Fas and also contains a death domain — and causes the accumulation of autoreactive T cells.

The 2.0 Å crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals a fold similar to that of tyrosine hydroxylase. It provides the first structural view of where mutations occur and a rationale to explain molecular mechanisms of the enzymatic phenotypes in the autosomal recessive disorder phenylketoneuria.

Every residue of a putative transmembrane helix in diacylglycerol kinase can be converted to both alanine and leucine while maintaining high specific activity, indicating that some transmembrane helices play a relatively passive role in structure and function.

Here we show how Mg²⁺ and Mn²⁺ function in Escherichia coli phosphoenolpyruvate carboxykinase (PCK) and we propose a general model for the role of binuclear metal clusters in enzyme-catalyzed phosphoryl-transfer reactions.

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 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 crystal structure of human replication and transcription cofactor PC4_CTD 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.

The 2.7 Å structure of the tetanus neurotoxin receptor binding fragment H_C reveals a jelly-roll domain and a β-trefoil domain. H_C retains the unique transport properties of the holotoxin and is capable of eliciting a protective immunological response against the full length holotoxin.