Correspondence in 1997

The three-dimensional structure of staphylokinase has been determined at 1.8 Å.The puntative site of interaction with plasminogen was identified and epitopes were mapped.

Based on structures of five mutants of green fluorescent protein (GFP), we describe two conformational variants with differing charge distribution that explain the published absorption and fluorescence spectra of GFP mutants.

Actophorin is a member of the actin-depolymerizing factor/cofilin family. It severs act in filaments and sequesters actin monomers. The crystal structure of actophorin will help to elucidate actin–ADF/cofilin interactions.

The specific binding of N⁷-methylguanine cap analogues to the RNA methyltransferase VP39 was observed through X-ray crystallography, providing a prototypical structure for a complex between a protein and an mRNA 5′ cap.

The electron crystallographic structure of the aquaporin-1 water channel, determined at ∼6Å, reveals that the protein has six transmembrane αhelices forming a trapezoid-like cylinder. There is a branched rod-like structure within the cylinder that traverses the membrane and likely contains at least one α-helix.

The structure of human heparin binding protein reveals that the serine proteinase fold has been used as a scaffold for a multifunctional protein with antibacterial activity, monocyte and T-cell activating properties and endotoxin and heparin binding capacity.

We report the solution structure of the 37,500 M_r carbohydrate-binding B subunit of verotoxin VT-1 (VTB) from enterohemorrhagic E. coli, which in contrast to the crystal structure is a symmetric homopentamer in solution.

Evidence is presented indicating that processive synthesis by HIV-1 reverse transcriptase involves interactions between the minor groove of the template-primer and a discrete protein structural element, the minor groove binding track (MGBT).

NMR studies of the δ subunit of the Escherichia coli F₁F₀-ATPsynthase reveal that it consists of an N-terminal six α-helix bundle and a less well ordered C terminus. Both domains are part of one of two separate connections between F₁ and F₀.

The three-dimensional structure of the calponin homology domain present in many actin binding cytoskeletal and signal-transducing proteins has been determined at 2.0 Å resolution.

Phytase is a high molecular weight acid phosphatase. The structure has an α/β-domain similar to that of rat acid phosphatase and an α-domain with a new fold.

The NMR structure of an autonomously folding subdomain from villin headpiece is reported. It forms a novel three helix structure with the actin-binding residues arrayed on the C-terminal helix.

The three-dimensional structure of actively transcribing rotavirus particles reveals that the nascent mRNA transcripts generated within the core of the virion by endogenous transcriptase complexes are translocated through the intact capsid through a system of channels at the icosahedral five-fold axes.

The RecA protein forms a hexameric ring that is similar to the core of the F1-ATPase. Several lines of evidence suggest that this hexamer may be a structural homologue of ring helicases.

The crystal structure of a PNA duplex reveals both a right- and a left-handed helix in the unit cell. The helices are wide (28 Å), large pitched (18 bp) with the base pairs perpendicular to the helix axis, thereby demonstrating that PNA besides adapting to oligonucleotide partners also has a unique structure by itself.

The high resolution structure of the new therapeutic target, cathepsin K, complexed with the potent mechanism-based inhibitor, APC3328, reveals the substrate-binding sites of this cysteine proteinase and validates the binding mode for this inhibitor class.

The structure of human cathepsin K, a potential target for treatment of osteoporosis, reveals active site differences with homologous cysteine proteinases that should enable the design of cathepsin K selective inhibitors.

Kinetic and spectroscopic evidence show that certain bZIP peptides favour a DMA binding mechanism in which monomers sequentially assemble into a dimer at their DMA target site.

Electron cryo-microscopy and image analysis of frozen-hydrated, two-dimensional crystals of gap junction membrane channels formed by recombinant α₁ connexin (Cx43) reveal a ring of transmembrane α-helices that lines the aqueous pore and a second ring of α-helices in close contact with the membrane lipids.