The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section D: Biological Crystallography.
See also Forthcoming articles in all IUCr journals.
Synopsis: structural analysis of apo and DNA-bound HU from Staphylococcus aureus (SHU) revealed that conformational changes occur in both the protein and DNA upon DNA binding. Base readout and shape readout mechanisms are involved in DNA binding and recognition by SHU, in which -arm flexibility is a major determinant.
Synopsis: The structures of retinal-bound and retinol-bound hCRBPII are reported. The X-ray flux and wavelength-dependent rearrangement of retinol in the hCRBPII binding pocket is demonstrated. The binding modes of retinol and retinal in CRBPI and CRBPII are contrasted.
Synopsis: Structural and enzymological characterization of the human degradative medium chain specific 3-ketoacyl-CoA thiolase (hT1) shows that the structure is highly similar to the short-chain specific tetrameric biosynthetic thiolases, except for small structural differences in two loops at the active site, providing extra space for a medium chain fatty acyl tail to bind. The intrinsic thioesterase activity of hT1 is also discussed.
Synopsis: Crystal structures of P. vivax serine hydroxymethyltransferase (PvSHMT) in complex with L-serine and with D-serine and 5-formyltetrahydrofolate provide better understanding of ligand binding and the catalytic mechanism. Features that are important for controlling the activity and specificity of PvSHMT such as stereoselectivity and redox status are addressed.
Synopsis: The atomic resolution X-ray diffraction structure of the reduced state of the redox flavoenzyme cholesterol oxidase is presented. The structure indicates the presence of an H atom bound to the flavin N5, suggesting that a hydride transfer has occurred.
Synopsis: The variable C-terminal tail of manganese peroxidases, a group of enzymes involved in lignin degradation, is implicated in their catalytic and stability properties, as shown by new crystal structures, molecular-simulation and directed-mutagenesis data. Based on this structural-functional evaluation, short and long/extralong manganese peroxidase subfamilies have been accepted; the latter are characterized by exceptional stability, while it is shown for the first time that the former are able to oxidize other substrates at the same site where manganese(II) is oxidized.
Synopsis: Crystal structures of the wild type and the N253A mutant of trehalose synthase from D. radiodurans in complex with the inhibitor Tris have been determined at 2.7 and 2.21 Å resolution, respectively, and they display a closed conformation for catalysis of the intramolecular isomerization.
Synopsis: Structures of EphA2 representing three activation states reveal that EphA2 probably possesses an alternate activation mechanism distinct from those of other Eph receptor tyrosine kinases.
Synopsis: Evolutionary comparisons suggest that Cwc27 evolved from a prolyl isomerase to a pure proline binder. The increase in the thermal stability of the PPIase domain of Cwc27 from C. thermophilum compared with its human counterpart is based on the additive effects of several amino-acid changes, which result in the removal of long side chains in strained conformations and additional intramolecular interactions.
Synopsis: The advantages of perdeuteration with regard to solvent visibility in macromolecules is demonstrated through the comparison of two neutron protein structures.
Synopsis: Two crystal forms of eIF5B and one crystal form of the eIF5B-eIF1A complex exhibit four different conformations of eIF5B, indicating that the conformation of eIF5B is highly flexible. The interaction between eIF5B domain IV and the eIF1A C-terminal tail may restrict the flexibility of eIF5B on the ribosome and stabilize the interface for ribosome subunit joining.
Synopsis: The crystal structure of a novel human norovirus polymerase replication complex reveals changes in conformation similar to a state following nucleotide incorporation.
Synopsis: The maximum-likelihood free-kick target, which calculates model error estimates from the work set and a randomly displaced model, proved superior in the accuracy and consistency of refinement of crystal structures compared with the maximum-likelihood cross-validation target, which calculates error estimates from the test set and the unperturbed model.
Synopsis: The ISPyB information-management system for crystallography has been adapted to include data from small-angle X-ray scattering of macromolecules in solution experiments.
Synopsis: The Collaborative Computational Project for Electron cryo-Microscopy (CCP-EM) is a new initiative for the structural biology community, following the success of CCP4 for macromolecular crystallography. Progress in supporting the users and developers of cryoEM software is reported.
Synopsis: The biophysical characterization of protein-ligand interactions in solution using techniques such as thermal shift assay, or on surfaces using, for example, dual polarization interferometry, plays an increasingly important role in complementing crystal structure determinations.
Copyright © International Union of Crystallography