4QQ8: Crystal Structure Of The Formolase Fls In Space Group P 43 21 2

Citation:
Abstract
We describe a computationally designed enzyme, formolase (FLS), which catalyzes the carboligation of three one-carbon formaldehyde molecules into one three-carbon dihydroxyacetone molecule. The existence of FLS enables the design of a new carbon fixation pathway, the formolase pathway, consisting of a small number of thermodynamically favorable chemical transformations that convert formate into a three-carbon sugar in central metabolism. The formolase pathway is predicted to use carbon more efficiently and with less backward flux than any naturally occurring one-carbon assimilation pathway. When supplemented with enzymes carrying out the other steps in the pathway, FLS converts formate into dihydroxyacetone phosphate and other central metabolites in vitro. These results demonstrate how modern protein engineering and design tools can facilitate the construction of a completely new biosynthetic pathway.
PDB ID: 4QQ8Download
MMDB ID: 127654
PDB Deposition Date: 2014/6/26
Updated in MMDB: 2015/04
Experimental Method:
x-ray diffraction
Resolution: 2.88  Å
Source Organism:
Similar Structures:
Biological Unit for 4QQ8: tetrameric; determined by author and by software (PISA)
Molecular Components in 4QQ8
Label Count Molecule
Proteins (4 molecules)
4
Formolase
Molecule annotation
Chemicals (12 molecules)
1
4
2
4
3
4
* Click molecule labels to explore molecular sequence information.

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