9s0t

Superfolder green fluorescent protein (sfGFP) exhibiting p-(phenylazo)-L-phenylalanine (Pap) at position 39 in complex with alpha-cyclodextrin

spinqualitylabelsall models 9s0t, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9s0t is a 2 chain structure with sequence from Aequorea victoria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.05Å Ligands: CRO, GLC, GOL, OZW Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin. Publication Abstract from PubMed Azobenzene derivatives, which show light-induced reversible trans<-->cis isomerization, have gained increasing attention in the area of protein science. p-(Phenylazo)-L-phenylalanine (Pap) was recently employed to enable the light-controlled affinity purification of biosynthetic proteins as part of the Azo-tag. Specific supramolecular complex formation with immobilized alpha-cyclodextrin (alpha-CD) groups is mediated by the Pap side chain in its low-energy trans-configuration, whereas photoisomerization to the cis-state leads to immediate dissociation. Here, we describe the X-ray crystallographic analysis of super-folder green fluorescent protein (sfGFP) displaying Pap at amino acid position 39 on its surface in complex with alpha-CD. While this experimental structure generally confirms the mode of host-guest interaction predicted by molecular modeling, there are two unexpected observations: (i) the conically shaped alpha-CD binds with its narrow end toward the aminoacyl moiety of Pap, despite appearing sterically more demanding, and (ii) the azobenzene side chain shows a considerably twisted conformation of its two phenyl rings, which contrasts with the fully coplanar arrangement usually anticipated for unmodified azobenzene and its chemical derivatives. Thus, this crystal structure of the photoswitchable noncanonical amino acid Pap (also known as AzoF or AzoPhe) provides valuable insight for future molecular engineering endeavors to endow proteins with light-controllable functions. Structural Basis of the Light-Switchable Interaction between an Azobenzene Side Chain in a Biosynthetic Protein and alpha-Cyclodextrin.,Eichinger A, Mayrhofer P, Anneser MR, Jarzinka L, Skerra A ChemistryOpen. 2026 Jan;15(1):e202500471. doi: 10.1002/open.202500471. Epub 2025 , Nov 19. PMID:41255130 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA