4QQ8

Crystal structure of the formolase FLS in space group P 43 21 2

Summary for 4QQ8

• Entry DOI: 10.2210/pdb4qq8/pdb
• Related: 4QPZ
• Descriptor: Formolase, MAGNESIUM ION, THIAMINE DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: formaldehyde lyase, lyase
• Biological source: Pseudomonas fluorescens
• Total number of polymer chains: 4
• Total formula weight: 247817.48

Authors

Shen, B.W.,Siegel, J.B.,Stoddard, B.L. (deposition date: 2014-06-26, release date: 2015-03-11, Last modification date: 2023-09-20)

Primary citation

Siegel, J.B.,Smith, A.L.,Poust, S.,Wargacki, A.J.,Bar-Even, A.,Louw, C.,Shen, B.W.,Eiben, C.B.,Tran, H.M.,Noor, E.,Gallaher, J.L.,Bale, J.,Yoshikuni, Y.,Gelb, M.H.,Keasling, J.D.,Stoddard, B.L.,Lidstrom, M.E.,Baker, D.
Computational protein design enables a novel one-carbon assimilation pathway.
Proc.Natl.Acad.Sci.USA, 112:3704-3709, 2015

PubMed 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.

PubMed: 25775555
DOI: 10.1073/pnas.1500545112

Experimental method

X-RAY DIFFRACTION (2.88 Å)