4AYG

Lactobacillus reuteri N-terminally truncated glucansucrase GTF180 in orthorhombic apo-form

Summary for 4AYG

• Entry DOI: 10.2210/pdb4ayg/pdb
• Descriptor: GLUCANSUCRASE, CALCIUM ION, GLYCEROL, ... (7 entities in total)
• Functional Keywords: transferase, glycosyltransferase, glycosyl hydrolase family 70, circularly permuted beta-alpha barrel
• Biological source: LACTOBACILLUS REUTERI
• Total number of polymer chains: 2
• Total formula weight: 241534.78

Authors

Pijning, T.,Vujicic-Zagar, A.,Kralj, S.,Dijkhuizen, L.,Dijkstra, B.W. (deposition date: 2012-06-21, release date: 2013-07-03, Last modification date: 2023-12-20)

Primary citation

Pijning, T.,Vujicic-Zagar, A.,Kralj, S.,Dijkhuizen, L.,Dijkstra, B.W.
Flexibility of Truncated and Full-Length Glucansucrase Gtf180 Enzymes from Lactobacillus Reuteri 180.
FEBS J., 281:2159-, 2014

PubMed Abstract: Glucansucrase enzymes synthesize high-molecular-mass extracellular α-glucan polysaccharides from sucrose. Previously, the crystal structure of truncated glucansucrase glucosyltransferase (GTF)180-ΔN from Lactobacillus reuteri 180 (lacking the N-terminal domain) revealed an elongated overall structure with two remote domains (IV and V) extending away from the core. By contrast, a new crystal form of the α-1,6/α-1,3 specific glucansucrase GTF180-ΔN shows an approximate 120(o) rotation of domain V about a hinge located between domains IV and V, giving a much more compact structure than before. Positional variability of domain V in solution is confirmed by small angle X-ray scattering experiments and rigid-body ensemble calculations. In addition, small angle X-ray scattering measurements of full-length GTF180 also provide the first structural data for a full-length glucansucrase, showing that the enzyme has an almost symmetric boomerang-like molecular shape, with a bend likely located between domains IV and V. The ~ 700-residue N-terminal domain, which is not present in the crystal structures, extends away from domain V and the catalytic core of the enzyme. We conclude that, as a result of the hinge region, in solution, GTF180-ΔN (and likely also the full-length GTF180) shows conformational flexibility; this may be a general feature of GH70 glucansucrases.

PubMed: 24597929
DOI: 10.1111/FEBS.12769

Experimental method

X-RAY DIFFRACTION (2 Å)