7vnl

Sandercyanin mutant-F55A-Biliverdin complex

spinqualitylabelsall models 7vnl, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.93Å Ligands: BLA, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Biliverdin IXalpha (BV) binds to several prokaryotic and eukaryotic proteins. How nature exploits the versatility of BV's properties is not fully understood. Unlike free BV, the Sandercyanin fluorescent protein bound to BV (SFP-BV) shows enhanced red fluorescence (675 nm) on excitation in the UV region (380 nm). Site-directed mutagenesis showed that the BV complex of two SFP variants, F55A and E79A, resulted in the loss of red fluorescence. Crystal structures of the complexes of these proteins with BV show the absence of stacking interactions of the F55 phenyl ring with BV. BV changes from ZZZssa conformation in the wild-type to ZZZsss conformation in the variants. In the nonfluorescent mutants, the lowest excited state is destabilized, resulting in nonradiative decay. Phenylalanine stacking enhances the red fluorescence of biliverdin IXalpha on UV excitation in sandercyanin fluorescent protein.,Yadav K, Ghosh S, Barak A, Schaefer W, Subramanian R FEBS Lett. 2022 Mar;596(6):796-805. doi: 10.1002/1873-3468.14281. Epub 2022 Jan, 17. PMID:35020202 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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