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X-ray structures reveal single-stranded DNA binding domains related to the OB-fold in human replication protein A (RPA) and human mitochondrial SSB protein (HmtSSB). These similarities may imply a common origin.
Indentifing the first genetic molecule will provide the key to understanding the origin of life. RNA is an unlikely candidate but peptide nucleic acid looks promising in the role of primordial genetic material.
Structures for three modular elements of actin-binding proteins provide hints of the deeper architectural principles governing the cortex of the eukaryotic cell.
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.
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.
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.
We report the solution structure of the 37,500 Mr 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.
