issue contents

ISSN: 2053-230X

December 2021 issue

Highlighted illustration

Cover illustration: Structure of mitogen-activated protein kinase kinase 1 in the DFG-out conformation [Nakae et al. (2021), Acta Cryst. F77, 459–464]. Eukaryotic protein kinases contain an Asp-Phe-Gly (DFG) motif, the conformation of which is involved in controlling the catalytic activity and can be switched between active-state (DFG-in) and inactive-state (DFG-out) conformations. The mechanism of conformational change is poorly understood, partly because there are few reports of the DFG-out conformation. Here, a novel crystal structure of nonphosphorylated human mitogen-activated protein kinase kinase 1 complexed with ATP-γS is reported in which MEK1 adopts the DFG-out conformation.


research communications

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This article reports the structure of the oligoribonuclease from Vibrio cholerae with a peptide derived from an N-terminal expression tag bound in the dinucleotide-binding pocket.

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Structural analyses of O6-methylguanine-DNA methyltransferases (MGMTs) and their mutants suggest that the highly conserved tyrosine at the N-terminus of the helix–turn–helix motif may play a protective role in MGMTs by preventing oxidants from entering the active site.

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Crystals of actophorin were grown in microgravity in an interactive process with astronauts on the International Space Station. Although the diffraction was not improved compared with crystals grown on Earth, a conformational change suggestive of motions intrinsic to actophorin function was observed.

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A crystal structure of nonphosphorylated mitogen-activated protein kinase kinase 1 (MEK1) complexed with ATP-γS is reported in which MEK1 adopts the DFG-out conformation.

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The X-ray structure of juvenile hormone diol kinase from the silkworm Bombyx mori has been determined at a resolution of 2.0 Å with an R factor of 19.0% and an Rfree of 24.8%. It is likely that the structure represents the calcium-inhibited form of this triple-EF-hand enzyme.

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The structures of four novel crystal forms of Satellite tobacco mosaic virus that were grown from a variety of salts are reported. These showed that while ammonium sulfate and sodium chloride preserve the structure of the genomic RNA, sodium bromide and sodium nitrate cause it to be disordered or lost. The structures also suggest that fivefold vertices of the virus may serve as ion channels.
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