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May 2017 issue
Cover illustration: The first plant acyl-CoA-binding protein structures: the close homologues OsACBP1 and OsACBP2 from rice (Guo et al., p. 438). The predicted ligand-binding site in OsACBP2 compared with the actual site in human liver ACBP. OsACBP2 molecule A and human liver ACBP are displayed as pale-gold and ice-blue ribbons, respectively; the ligand (C1 myristoyl-CoA) of human liver ACBP is shown as a ball-and-stick model. The predicted binding cavity of OsACBP2 is shown as a green patch and overlaps with a large part of the acyl chain of the myristoyl-CoA.
research papers
A series of diffraction data sets with increasing absorbed radiation dose were collected from a single crystal of Steccherinum murashkinskyi laccase at 1.35 Å resolution. The mechanism of oxygen reduction catalyzed by laccases is discussed.
PDB references: Steccherinum murashkinskyi laccase, 3 min exposure, 5mej; 33 min exposure, 5mew; 63 min exposure, 5mhu; 93 min exposure, 5mhv; 123 min exposure, 5mhw; 153 min exposure, 5mhx; 183 min exposure, 5mhy; 213 min exposure, 5mhz; 243 min exposure, 5mi1; 273 min exposure, 5mi2; 303 min exposure, 5mia; 333 min exposure, 5mib; 363 min exposure, 5mic; 393 min exposure, 5mid; 423 min exposure, 5mie; 453 min exposure, recooled crystal, 5mig
The NS3s of Dengue virus serotypes 2 and 4 are elongated and dynamic in solution. The protease domain of NS3 undergoes substantial conformational alterations owing to RNA binding. The interactions and effects of quercetin binding in NS3 are described.
The structure of the family B DNA polymerase from the hyperthermophilic archaeon P. calidifontis has been determined with an R factor of 24.47% and an Rfree of 28.81% at 2.80 Å resolution. The enzyme has a number of unique structural features which distinguish it from other archaeal DNA polymerases.
PDB reference: DNA polymerase, 5mdn
Structural analysis of an isoleucine 2-epimerase from L. buchneri provided new insight into the catalytic mechanism of bacterial fold-type I racemases.
The first structures of plant acyl-CoA-binding proteins, from rice, show similarity to the human liver and bovine homologues.
A new method called Pepsi-SAXS is presented that calculates small-angle X-ray scattering profiles from atomistic models. The method is based on the multipole expansion scheme and is significantly faster compared with the CRYSOL, FoXS and three-dimensional Zernike methods.
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