virusMED (Virus Metal binding sites, Epitopes and Drug binding sites) is a rich internet application based on a database of atomic interactions around hotspots in 7041 experimentally determined viral protein structures.

In eight of the nine crystal structures of M. smegmatis MutT1 reported here, an arrangement is observed in which domain 1 of one molecule and domain 2 of a neighbouring molecule (trans domain 2) are brought into close proximity, with ligand-binding sites at the interface between the two domains. This and other structural observations, along with biochemical results, lead to a plausible proposal for the mechanism of action of the enzyme.

The crystal structure of starch synthase I from barley was refined to 2.7 Å resolution. It includes a regulatory disulfide and a bound oligosaccharide. Activity assays were performed on several mutants.

This paper presents a survey of techniques that explore the surface properties of protein:protein interfaces so as to inform the prediction of probable sites of protein:protein interaction on newly determined protein structures.

The structure of the new class of controller proteins (exemplified by C.Csp231I) in complex with its 21 bp DNA-recognition sequence is presented, and the molecular basis of sequence recognition in this class of proteins is discussed. An unusual extended spacer between the dimer binding sites suggests a novel interaction between the two C-protein dimers.

The dimeric structure of Sfh3 (Sec14 family homologue 3 in yeast) is reported for the first time and differs from the Sec14 proteins reported to date, all of which are monomeric.

The crystal structure of the effector-binding domain of the transcriptional repressor AraR from B. subtilis in complex with the effector molecule (L-arabinose) was determined at 2.2 Å resolution. A detailed analysis of the crystal identified a dimer organization that is distinctive from that of other members of the GalR/LacI family.

Structures of orthorhombic crystals of lysozyme at pH 4.5 show that the binding of phosphate ions produces long-range conformational changes and that low humidity produces a displacement of the fifth α-helix towards the active-site cavity. The interaction of some anions must be considered when analysing experiments with lysozyme at acidic pH values.

The crystal structures of adenylylated and unadenylylated GlnK, a P_II protein from Corynebacterium glutamicum, indicate that adenylylation of Tyr51 in the T-loop does not interfere with the P_II-typical conformational changes that occur in the T-loop upon effector binding. Rather, T-loop adenylylation further expands the repertoire of mechanisms that enable P_II function.

In the course of soaking experiments of lytic polysaccharide monooxygenase crystals with potential oligosaccharide ligands, local changes in crystal packing, various degrees of active-site disorder and binding of oligosaccharides at potential branching or surface binding sites were observed.