4J9J

Structure of designed HisF

Summary for 4J9J

• Entry DOI: 10.2210/pdb4j9j/pdb
• Descriptor: Imidazole glycerol phosphate synthase subunit HisF (2 entities in total)
• Functional Keywords: beta barrel, protein engineering, lyase
• Biological source: Thermotoga maritima; More
• Cellular location: Cytoplasm: Q9X0C6
• Total number of polymer chains: 1
• Total formula weight: 26326.29

Authors

Sterner, R.,Rajendran, C.,Sperl, J. (deposition date: 2013-02-16, release date: 2013-07-17, Last modification date: 2023-09-20)

Primary citation

Sperl, J.M.,Rohweder, B.,Rajendran, C.,Sterner, R.
Establishing catalytic activity on an artificial ( beta alpha )8-barrel protein designed from identical half-barrels.
Febs Lett., 587:2798-2805, 2013

PubMed Abstract: It has been postulated that the ubiquitous (βα)8-barrel enzyme fold has evolved by duplication and fusion of an ancestral (βα)4-half-barrel. We have previously reconstructed this process in the laboratory by fusing two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF). The resulting construct HisF-CC was stepwise stabilized to Sym1 and Sym2, which are extremely robust but catalytically inert proteins. Here, we report on the generation of a circular permutant of Sym2 and the establishment of a sugar isomerization reaction on its scaffold. Our results demonstrate that duplication and mutagenesis of (βα)4-half-barrels can readily lead to a stable and catalytically active (βα)8-barrel enzyme.

PubMed: 23806364
DOI: 10.1016/j.febslet.2013.06.022

Experimental method

X-RAY DIFFRACTION (2.3 Å)