Probing the Allosteric Regulation of the
            <i>Agrobacterium tumefaciens</i>
            ADPGlucose Pyrophosphorylase

Bains, Gagandeep; Böhmer, Nadine; Sanders, Jamie; Guzmán, David Calderón; Meyer, Christopher R.

doi:10.1096/fasebj.25.1_supplement.765.3

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“…For example, a strong correlation can be made between the specificity of a bacterial organism's BE, the structure of its glycogen, the relative digestibility of the glycogen, and the organism's propensity to live in harsher, less nutrient-rich environments [6,12,13]. A number of studies have shed light on this relationship in a wide variety of bacterial organisms, including E. coli [14,15], Synechocystis [16], Agrobacterium tumefaciens [17], Rhodococcus [18], Vibrio vulnificus [19,20], and Galdieria sulphuraria [21,22]. Branching enzymes have also found use in a number of commercial applications, and branch transfer length is of key importance in these applications as well [23].…”

Section: Introductionmentioning

confidence: 99%

The Structure of Maltooctaose-Bound Escherichia coli Branching Enzyme Suggests a Mechanism for Donor Chain Specificity

Fawaz,

Bingham,

Nayebi

et al. 2023

Molecules

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Glycogen is the primary storage polysaccharide in bacteria and animals. It is a glucose polymer linked by α-1,4 glucose linkages and branched via α-1,6-linkages, with the latter reaction catalyzed by branching enzymes. Both the length and dispensation of these branches are critical in defining the structure, density, and relative bioavailability of the storage polysaccharide. Key to this is the specificity of branching enzymes because they define branch length. Herein, we report the crystal structure of the maltooctaose-bound branching enzyme from the enterobacteria E. coli. The structure identifies three new malto-oligosaccharide binding sites and confirms oligosaccharide binding in seven others, bringing the total number of oligosaccharide binding sites to twelve. In addition, the structure shows distinctly different binding in previously identified site I, with a substantially longer glucan chain ordered in the binding site. Using the donor oligosaccharide chain-bound Cyanothece branching enzyme structure as a guide, binding site I was identified as the likely binding surface for the extended donor chains that the E. coli branching enzyme is known to transfer. Furthermore, the structure suggests that analogous loops in branching enzymes from a diversity of organisms are responsible for branch chain length specificity. Together, these results suggest a possible mechanism for transfer chain specificity involving some of these surface binding sites.

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