ArticleActa crystallographica. Section F, Structural biology communications2025
Biochemical characterization and preliminary X-ray crystallographic analysis of cyanobacterial α-glucan phosphorylases.
Article in Acta crystallographica. Section F, Structural biology communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Several cyanobacterial species, including Crocosphaera subtropica ATCC 51142, accumulate cyanobacterial starch instead of glycogen, although nearly all cyanobacteria accumulate glycogen. The glycogen-producing Synechococcus elongatus PCC 7942 possesses one α-glucan phosphorylase (Pho) isozyme, whereas strain 51142 has three Pho isozymes. Based on their primary structures, these enzymes belong to glycosyl transferase (GT) family 35, with the cyanobacterial GT35-type Phos further subdivided into types I-III. In this study, to elucidate the significance of the coexistence of multiple GT35-type Pho isozymes, those from strain 51142 (type I, cce_1629; type II, cce_1603 and cce_5186) and strain 7942 (type I, Synpcc7942_0244) were overexpressed in Escherichia coli and biochemically characterized. All isozymes catalysed the phosphorolysis and reverse phosphorolysis reactions. The type I isozyme from a cyanobacterial starch-producing strain (cce_1629) differed in substrate specificity and specific activity compared with the others. The behaviour towards the effectors (AMP and ATP) of the type I and type II isozymes differed from each other. These findings enhance our understanding of the roles of cyanobacterial Pho isozymes in α-glucan metabolism. Furthermore, recombinant cce_1603 was crystallized using the hanging-drop vapour-diffusion method. Crystals were obtained at 293 K in the presence of 10 mM maltoheptaose, 45%(w/v) PEG 400, 0.1 M Tris-HCl pH 8.0, 0.2 M lithium sulfate. The crystals belonged to space group R32 (hexagonal setting) with unit-cell parameters a = b = 267.23, c = 204.43 Å, and diffracted to beyond 2.70 Å resolution. Matthews coefficient calculations indicated the presence of two molecules in the asymmetric unit. Structural determination is currently under way. The crystal structure of cce_1603 will aid in the understanding of the structural basis of cyanobacterial GT35-type Pho isozymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.