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September 2024 issue
research communications
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Brucella ovis leucine-, isoleucine-, valine-, threonine- and alanine-binding protein structures have a prototypical bacterial periplasmic amino acid-binding protein topology with a conformationally flexible peptide-binding cavity in the absence of peptide.
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The crystal structure determination of CdaA enzymes from Streptococcus pneumoniae, Bacillus subtilis and Enterococcus faecium is reported. Additionally, the structural results of a fragment screen of B. subtilis CdaA are presented, along with a subsequent in silico drug-repurposing screen conducted using the OpenEye suite.
PDB references: Streptococcus pneumoniae CdaA, 8ofh; Enterococcus faecium CdaA, 8ofo; Bacillus subtilis CdaA, 8ogm; complex with fragment A09, 8ogn; complex with fragment A12, 8ogo; complex with fragment B03, 8ogp; complex with fragment B06, 8ogq; complex with fragment B07, 8ogr; complex with fragment B08, 8ogs; complex with fragment C04, 8ogt; complex with fragment C07, 8ogu; complex with fragment C08, 8ogv; complex with fragment D02, 8ogw; complex with fragment D04, 8ogy; complex with fragment D06, 8ogz; complex with fragment D08, 8oh0; complex with fragment E04, 8oh1; complex with fragment E08, 8ohb; complex with fragment E12, 8ohc; complex with fragment F03, 8ohe; complex with fragment F04, 8ohf; complex with fragment F09, 8ohg; complex with fragment G05, 8ohh; complex with fragment G08, 8ohj; complex with fragment H01, 8ohk; complex with fragment H09, 8ohl; complex with fragment H11, 8oho; complex with Compound 7, 9g0g
Protein tyrosine phosphatase non-receptor type 2 (PTPN2), a known target for cancer immunotherapy, was crystallized with novel crystal packing, resulting in a true apo PTPN2 crystal structure with an unbound active site. Inhibitor-bound PTPN2 crystal structures were obtained by soaking these apo crystals with an active-site inhibitor and an allosteric inhibitor.
The crystal structure of GDP-bound human M-RAS protein is presented with two forms of crystal packing.
The high-resolution structure of a Rib domain derived from L. reuteri reveals a significant structural variant of the canonical Ig-like fold.