issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

July 2024 issue

Highlighted illustration

Cover illustration: A pectin-active family 1 polysaccharide lyase from Pseudoalteromonas fuliginea [Hobbs & Boraston (2024), Acta Cryst. F80, 142–147]. This recently identified marine bacterium has extensive enzymatic machinery to metabolize polysaccharides, and here the first structural insight into a pectinase of marine origin and the first structure of a PL1 enzyme in subfamily 2 are presented.

research communications


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A crystal of the N-terminal domain of hypothetical protein Rv1421 from Mycobacterium tuberculosis H37Rv (MtRv1421-NTD) diffracted to 1.7 Å resolution. MtRv1421-NTD, which contains a Walker A/B-like motif, can bind uridine diphosphate (UDP) and UDP-N-acetylglucosamine, indicating that the presence of a UDP moiety on the ligand may be essential for its interaction.

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The structure of PfPL1, the first structure of a polysaccharide lyase family 1 subfamily 2 enzyme, reveals a parallel β-helix fold. Structural comparisons reveal insights into substrate recognition and key elements in the catalytic machinery.

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The crystal structure of the FERM domain of protein tyrosine phosphatase non-receptor type 21, a regulator of cancer progression and invasion, was determined and an atomic-level structural analysis was conducted.

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Complementary-determining region 3 (CDR3) of the light chain interacts with the extended CDR3 of the paired heavy chain in bovine ultralong antibodies. Exchanging light chains between two different ultralong antibodies induced a small axial twist in the CDR3H β-ribbon stalk region; however, comparative crystallographic interface analysis indicates that the ultralong loops have flexibility and their positioning is affected by crystal packing.
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