issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

September 2016 issue

Highlighted illustration

Cover illustration: Halobacterium salinarum halorhodopsin with a partially depopulated primary chloride-binding site (Schreiner et al., p. 692). Halophilic archaea such as H. salinarum thrive in highly saturated brines. In order to maintain the osmotic balance, the transmembrane pump halorhodopsin translocates chloride ions from the extracellular to the cytoplasmic side upon illumination. Here, to further elucidate this ion-transport mechanism at the molecular level, crystals have been treated to provoke the loss of chloride.

research communications


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The study of the crystal structure of proplasmepsin IV from P. falciparum and its comparison with the structures of the mature enzyme and of other proplasmepsins show the flexibility that characterizes the aspartic protease zymogens from malaria parasites.

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The gene encoding a putative siderophore-interacting protein from the marine bacterium S. frigidimarina was successfully cloned, followed by expression and purification of the gene product. Optimized crystals diffracted to 1.35 Å resolution and preliminary crystallographic analysis is promising with respect to structure determination and increased insight into the poorly understood molecular mechanisms underlying iron acquisition.

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The C-terminal domain of the HsdR subunit of the E. coli type I restriction-modification system EcoR124I was purified and crystallized in form of a pHluorin (GFP) fusion protein and X-ray diffraction data were collected to a resolution of 2.45 Å.

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The large C-terminal domain of the C. crescentus surface-layer protein RsaA has been crystallized. Initial RsaA crystals have been shown to diffract to ∼2.5 Å resolution.

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A lactonase, named GcL, from G. caldoxylosilyticus has been isolated, purified, characterized and crystallized. Here, it is shown that GcL is a thermostable enzyme that is extremely proficient at degrading lactones. Its structure is expected to provide insights regarding the catalytic mechanism and to highlight the structural determinants involved in the high proficiency of this enzyme.

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The Vaccinia virus D4/A20 complex is the DNA polymerase cofactor. The heterodimer interface has been analysed using three new crystal structures of the complex in which key residues forming a cation–π interaction have been mutated.

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A structure of halorhodopsin with about 50% occupancy of its primary chloride-binding site showed no structural changes in the protein, suggesting that anion binding is not strictly coupled to protein conformation in this crystal form.

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The crystal structure of Z. palmae pyruvate decarboxylase was elucidated at 2.15 Å resolution.

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The crystal structures of complexes of the SH3 domain of the Fyn tyrosine kinase with the high-affinity peptides VSL12 (class I) and APP12 (class II) have been solved at 1.6 and 2.1 Å resolution, respectively. These structures support an important role of water molecules in facilitating conformational changes to allow binding of the proline-rich motifs in the two available orientations in this family of SH3 domains.

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The DNA-binding domain of SETMAR was successfully crystallized in a complex with its ancestral terminal inverted repeat and a variant of this sequence through a systematic approach, and initial Se SAD phasing was achieved through the judicious addition of Met residues.

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The structure of XC_3703, a YajQ-family protein and a potential c-di-GMP receptor, has been determined at 2.1 Å resolution.

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A crystal structure of ToxT at 1.65 Å resolution with a similar overall structure to the previously determined structure is reported. A region that extends from Asp101 to Glu110, which can influence ToxT activity but was disordered in the previous structure, can be traced entirely in the current structure.
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