8S7H
Fructose 6-phosphate aldolase (FSA) from Escherichia coli
Summary for 8S7H
| Entry DOI | 10.2210/pdb8s7h/pdb |
| EMDB information | 19772 |
| Descriptor | Fructose-6-phosphate aldolase 1 (1 entity in total) |
| Functional Keywords | fructose 6-phosphate aldolase, lyase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 10 |
| Total formula weight | 238956.72 |
| Authors | Hebert, H.,Widersten, M. (deposition date: 2024-03-01, release date: 2025-03-12, Last modification date: 2025-09-24) |
| Primary citation | Hebert, H.,Sonmez, E.,Purhonen, P.,Widersten, M. Structure of the iminium reaction intermediate in an engineered aldolase explains the carboligation activity toward arylated ketones and aldehydes. Structure, 32:1322-1326.e4, 2024 Cited by PubMed Abstract: Two structures of fructose 6-phosphate aldolase, the wild-type and an engineered variant containing five active-site mutations, have been solved by cryoelectron microscopy (cryo-EM). The engineered variant affords production of aldols from aryl substituted ketones and aldehydes. This structure was solved to a resolution of 3.1 Å and contains the critical iminium reaction intermediate trapped in the active site. This provides new information that rationalizes the acquired substrate scope and aids in formulating hypotheses of the chemical mechanism. A Tyr residue (Y131) is positioned for a role as catalytic acid/base during the aldol reaction and the different structures demonstrate mobility of this amino acid residue. Further engineering of this fructose 6-phosphate aldolase (FSA) variant, guided by this new structure, identified additional FSA variants that display improved carboligation activities with 2-hydroxyacetophenone and phenylacetaldehyde. PubMed: 39013461DOI: 10.1016/j.str.2024.06.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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