issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

June 2019 issue

Highlighted illustration

Cover illustration: Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus [Stroobants et al. (2019), Acta Cryst. F75, 428-434].

research communications


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The structure of Aspergillus aculeatus β-1,4-galactanase, a glycoside hydrolase belonging to family 53, has been determined in complex with galactobiose at subsites −1 and −2.

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Crystal structures of the extracellular domain of rabbit neprilysin and of neprilysin complexed with the inhibitors phosphoramidon or thiorphan are reported.

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The apo structure of the SPRY domain of human SPRY domain-containing SOCS box protein 2 (SPSB2) determined at 1.9 Å resolution shows that its inducible nitric oxide synthase (iNOS)-binding site is highly preformed and that the C-terminal His6 tag binds to a shallow pocket adjacent to the iNOS-binding site, which may help in structure-based and fragment-based SPSB2 inhibitor design.

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High-resolution structures of apocruzain and cruzain bound to S-methyl thiomethanesulfonate provide insights for the structure-based design of new cruzain inhibitors.

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The crystal structure of the 1-Cys peroxiredoxin from S. islandicus is presented; it assembles into a ring-shaped decamer composed of five homodimers. It is concluded that this Prx6-like protein undergoes decamerization independently of arm-domain cysteines.

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The growth of a large crystal of a potassium ion channel, and neutron and X-ray data collection from the crystal are described.

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The dimerization domain of splicing factor proline/glutamine-rich (SFPQ), an essential RNA-binding protein, has been crystallized in the C-centered orthorhombic space group C2221 with one monomer in the asymmetric unit, and its structure has been determined and refined to 1.9 Å resolution. The crystal structure was analyzed and compared with the solution scattering data.

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The crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus HB8 (TtThy1, TTHA1096) was determined in complex with FAD and phosphate at 2.5 Å resolution. TtThy1 is a tetrameric molecule, to which four FAD molecules are bound. Two phosphate ions were bound to each dUMP-binding site. The characteristic feature of TtThy1 is the existence of an extra C-terminal domain (CTD) consisting of three α-helices and a β-strand.

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Interferon-inducible protein 204 (p204) binds to microbial DNA to elicit inflammatory responses and induce interferon production. The DNA-binding affinity of the p204 HIN1 domain has been characterized and its crystal structure has been determined. Surface-charge distribution together with sequence alignment suggests that the p204 HIN domain uses its L12 and L45 loops for DNA binding.

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Human liver pyruvate kinase converts phosphoenolpyruvate to pyruvate in the final step of glycolysis and is allosterically activated by fructose-1,6-bisphosphate. The allosteric site is located between the phosphate-binding loop and the allosteric loop. The crystal structures of four site-directed mutants revealed a conformational toggle between the open and closed positions of the allosteric loop.
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