issue contents

ISSN: 2053-230X

May 2020 issue

Highlighted illustration

Cover illustration: The EF-hand protein MCFD2 complexed with the intracellular lectin ERGIC-53 involved in glycoprotein transport [Satoh et al. (2020), Acta Cryst. F76, 216-221]. The transmembrane intracellular lectin ER-Golgi intermediate compartment protein 53 (ERGIC-53) and the soluble EF-hand multiple coagulation factor deficiency protein 2 (MCFD2) form a complex that functions as a cargo receptor, trafficking various glycoproteins between the endoplasmic reticulum and the Golgi apparatus. Crystal structures of ERGIC-53CRD-MCFD2 complexes reveal that MCFD2, but not ERGIC-53-CRD, exhibits significant conformational plasticity that may be relevant to its accommodation of various polypeptide ligands.

research communications

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A single-chain, tailless Xenopus laevis H2A/H2B dimer construct (scH2BH2A) was engineered by directly fusing the C-terminus of H2B to the N-terminus of H2A without an artificial linker sequence. A high-resolution crystal structure of scH2BH2A shows that it adopts a nearly identical fold to that of nucleosomal H2A/H2B and may be useful for future structural studies of many H2A/H2B-interacting proteins.

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Insights were obtained into the structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway for the biosynthesis of lysine.

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The crystal structure of Pseudomonas aeruginosa Fis is composed of an N-terminal flexible loop and a C-terminal helix–turn–helix motif.

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The structure of the Pseudomonas aeruginosa T6SS PldB immunity protein PA5086 is reported at 1.9 Å resolution. Comparison of PA5086 with its homologs PA5087 and PA5088 showed great similarities in sequence and structure, but vast divergences in electrostatic potential surfaces.

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The crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum is reported. It has high structural similarity to other gluconate 5-dehydrogenase proteins, demonstrating that this enzyme is highly conserved.
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