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Search for a dextransucrase minimal motif involved in dextran binding
Author(s) -
Suwannarangsee Surisa,
Moulis Claire,
Potocki-Veronese Gabrielle,
Monsan Pierre,
Remaud-Simeon Magali,
Chulalaksananukul Warawut
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.062
Subject(s) - dextransucrase , leuconostoc mesenteroides , dextran , chemistry , dissociation constant , biochemistry , stereochemistry , biology , bacteria , lactic acid , receptor , genetics
Fourteen truncated forms of Leuconostoc mesenteroides NRRL B512‐F dextransucrase, involving N‐, C‐ or N‐ plus C‐terminal domain truncations were tested for their ability to bind dextrans. The shortest fragment (14 kDa molecular weight) that still exhibited a strong interaction with dextran was localized between amino acids N1397 and A1527 of the C‐terminal domain (GBD‐7) and consists of six YG repeats. With a dissociation constant K d of 2.8 × 10 −9 M, this motif shows a very high affinity for isomaltohexaose and longer dextrans, supporting the proposed role of GBD in polymer formation. The potential application of GBD‐7 as an affinity tag onto cheap resins like Sephacryl ® S300HR for rapid purification was evaluated and is discussed.