4j9j | pdb_00004j9j

Structure of designed HisF

spinqualitylabelsall models 4j9j, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4j9j is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HIS6_THEMA IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013] Publication Abstract from PubMed It has been postulated that the ubiquitous (betaalpha)8-barrel enzyme fold has evolved by duplication and fusion of an ancestral (betaalpha)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 (betaalpha)4-half-barrels can readily lead to a stable and catalytically active (betaalpha)8-barrel enzyme. Establishing catalytic activity on an artificial (betaalpha)-barrel protein designed from identical half-barrels.,Sperl JM, Rohweder B, Rajendran C, Sterner R FEBS Lett. 2013 Jun 24. pii: S0014-5793(13)00469-9. doi:, 10.1016/j.febslet.2013.06.022. PMID:23806364 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also IGPS 3D structures

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