5ZOL
Crystal structure of a three sites mutantion of FSAA complexed with HA and product
Summary for 5ZOL
| Entry DOI | 10.2210/pdb5zol/pdb |
| Descriptor | Fructose-6-phosphate aldolase 1, 1-hydroxypropan-2-one, (3S,4S)-3,4-dihydroxy-4-(thiophen-2-yl)butan-2-one, ... (7 entities in total) |
| Functional Keywords | fructose-6-phosphate aldolase, donor, acceptor, mutant, flexible, lyase |
| Biological source | Escherichia coli (strain K12) |
| Total number of polymer chains | 10 |
| Total formula weight | 272815.74 |
| Authors | Wu, L.,Yang, X.H.,Yu, H.W.,Zhou, J.H. (deposition date: 2018-04-13, release date: 2019-06-12, Last modification date: 2024-10-23) |
| Primary citation | Yang, X.,Wu, L.,Li, A.,Ye, L.,Zhou, J.,Yu, H. The engineering of decameric d-fructose-6-phosphate aldolase A by combinatorial modulation of inter- and intra-subunit interactions. Chem.Commun.(Camb.), 56:7561-7564, 2020 Cited by PubMed Abstract: The combinatorial modulation of inter- and intra-subunit interactions of decameric d-fructose-6-phosphate aldolase A (FSAA) generated a triple-site variant I31T/Q59T/I195Q FSAA with 27- to 278-fold improvement in activity towards target heteroaromatic aldehydes. X-ray crystallographic data and molecular dynamics simulations ascribed the enhanced activity to the pronounced flexibility of the interface region between subunits, the expanded substrate entrance and binding pocket, and enhanced proton transfer, unambiguously demonstrating the efficiency of this strategy for engineering multimeric enzymes. PubMed: 32519699DOI: 10.1039/d0cc02437f PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.172 Å) |
Structure validation
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