7ZC0
4,6-alpha-glucanotransferase GtfC from Geobacillus 12AMOR1
This is a non-PDB format compatible entry.
Summary for 7ZC0
| Entry DOI | 10.2210/pdb7zc0/pdb |
| Descriptor | 4,6-alpha-Glucanotransferase, GLYCEROL, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | 4, 6-alpha-glucanotransferase, gtfc, starch conversion, transferase |
| Biological source | Geobacillus |
| Total number of polymer chains | 1 |
| Total formula weight | 82507.81 |
| Authors | Pijning, T.,Dijkhuizen, L.,Guskov, A.,te Poele, E.M. (deposition date: 2022-03-25, release date: 2022-12-07, Last modification date: 2024-01-31) |
| Primary citation | Pijning, T.,Te Poele, E.M.,de Leeuw, T.C.,Guskov, A.,Dijkhuizen, L. Crystal Structure of 4,6-alpha-Glucanotransferase GtfC-Delta C from Thermophilic Geobacillus 12AMOR1: Starch Transglycosylation in Non-Permuted GH70 Enzymes. J.Agric.Food Chem., 70:15283-15295, 2022 Cited by PubMed Abstract: GtfC-type 4,6-α-glucanotransferase (α-GT) enzymes from Glycoside Hydrolase Family 70 (GH70) are of interest for the modification of starch into low-glycemic index food ingredients. Compared to the related GH70 GtfB-type α-GTs, found exclusively in lactic acid bacteria (LAB), GtfCs occur in non-LAB, share low sequence identity, lack circular permutation of the catalytic domain, and feature a single-segment auxiliary domain IV and auxiliary C-terminal domains. Despite these differences, the first crystal structure of a GtfC, GbGtfC-ΔC from 12AMOR1, and the first one representing a non-permuted GH70 enzyme, reveals high structural similarity in the core domains with most GtfBs, featuring a similar tunneled active site. We propose that GtfC (and related GtfD) enzymes evolved from starch-degrading α-amylases from GH13 by acquiring α-1,6 transglycosylation capabilities, before the events that resulted in circular permutation of the catalytic domain observed in other GH70 enzymes (glucansucrases, GtfB-type α-GTs). AlphaFold modeling and sequence alignments suggest that the GbGtfC structure represents the GtfC subfamily, although it has a so far unique alternating α-1,4/α-1,6 product specificity, likely determined by residues near acceptor binding subsites +1/+2. PubMed: 36442227DOI: 10.1021/acs.jafc.2c06394 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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