9rxf | pdb_00009rxf

E20K/N28G/V36L/D43K/Q48E/I59A/E61K/E72K/V76L/N79S/I92A/D126K/A142V/D153K/D154E/S158T FLAVODOXIN FROM ANABAENA

spinqualitylabelsall models 9rxf, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9rxf is a 2 chain structure with sequence from Nostoc sp. PCC 7119. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: FMN, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FLAV_NOSSO Low-potential electron donor to a number of redox enzymes. Publication Abstract from PubMed Enhancing the stability of highly stable proteins represents an interesting challenge in protein design. We have used the computational tool Protposer to rapidly achieve large additional stabilization of apoflavodoxin, a protein strongly thermostabilized over the years through protein engineering based on educated guesses. By rationally combining top-ranked mutations onto a previously stabilized variant (6 M), we have generated a series of new mutants and characterized their stability by thermal and chemical denaturation. Relative to the starting variant, the T(m) of 10 M apoflavodoxin is nearly 9 degrees C higher, while the simplified 3 M and 4 M mutants, showing improved refolding properties, display increases of 6/7.5 degrees C, respectively. The thermostabilizing effects of individual mutations are close to additive and translate into a large increase in conformational stability at 25.0 degrees C. Comparison of the x-ray structures of progressively stabilized WT, 6 M and 10 M flavodoxins reveals a concomitant mild trend toward shorter hydrogen bonds, reduced internal cavity volumes and narrower tunnels. Overall, these conformational changes are minor, and a functional assay confirms the mutants also preserve their catalytic activity. These findings demonstrate that even highly stable proteins can be further stabilized through rational design using a simple computational tool that automatically analyses PDB files and identifies stabilizing mutations. Protein thermostabilization with Protposer: Pushing the stability limits and folding reversibility of a highly-stabilized apoflavodoxin.,Hidalgo-Toledo A, Bazco D, Correa-Perez V, Martinez-Julvez M, Sancho J Int J Biol Macromol. 2025 Oct 15;331(Pt 1):148333. doi: , 10.1016/j.ijbiomac.2025.148333. PMID:41106744 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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