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. 2015 Jan 23;12:6. doi: 10.1186/s12977-014-0127-3

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© Moulaei et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Structure and binding site orientation of dimeric GRFT and mutations used to generate monomeric GRFT. Dimeric GRFT (A) is a domain-swapped dimer with two identical carbohydrate-binding domains (circled in blue) separated by 50 Å and at a relative angle of ~160° from each other. Obligate monomeric GRFT (B) was generated by the addition of Gly-Ser residues in the hinge region of wild-type GRFT. The enhanced flexibility of the hinge region resulted in the collapse of the swapped domain to form an obligate monomer, mGRFT.