issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

June 2021 issue

Highlighted illustration

Cover illustration: The minichromosome maintenance (MCM) complex forms a hexameric ring that unwinds DNA at the replication forks of all eukaryotes and archaea. The crystal structure of a dimer of the N-terminal domain of MCM from Sulfolobus solfataricus [Meagher et al. (2021), Acta Cryst. F77, 177–186] suggests a straightforward model for the action of the MCM ring.

research communications


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The crystal structure of the Thr316Ala mutant of Schizosaccharomyces pombe Sst2 reveals an increase in the flexibility of the Ins-1 turn, which prevents the formation of the closed conformation of the active site during catalysis. This indicates that Thr316 might be involved in tuning a precise level of dynamics by interacting with the key active-site flap residue Phe403, which is important for catalysis.

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Two nanobodies raised against the cytoplasmic domain of GldL were produced, their interaction with their target was characterized, and their crystal structures were solved.

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The minichromosome maintenance (MCM) complex forms a hexameric ring that unwinds DNA at the replication forks of all eukaryotes and archaea. The crystal structure of a dimer of the N-terminal domain of MCM from S. solfataricus with an intersubunit interface that is tighter than the interfaces observed in closed-ring crystal structures is presented. The altered intersubunit interface suggests a straightforward model for the MCM ring to open and permit DNA to pass through to fulfill critical steps that initiate DNA replication.

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An analytical assessment shows a preferential distribution of three space groups, i.e. P212121 > P1211 > C121, in soluble and membrane proteins as well as in their complexes. The distribution of these space groups also shows the same pattern whether a protein crystallizes with a monomer or an oligomer in the asymmetric unit. The results also indicate that the sizes of the two entities in the structures of soluble proteins crystallized as complexes do not influence the frequency distribution of space groups.
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