7RBW
Structure of Biliverdin-binding Serpin of Boana punctata (polka-dot tree frog)
Summary for 7RBW
| Entry DOI | 10.2210/pdb7rbw/pdb |
| Related | 1ATU |
| Descriptor | Biliverdin bindin serpin, BILIVERDINE IX ALPHA (3 entities in total) |
| Functional Keywords | serpin, biliverdin-binding serpin, near-infrared, fluorescent protein |
| Biological source | Boana punctata (Polka-dot tree frog, Hypsiboas punctatus) |
| Total number of polymer chains | 2 |
| Total formula weight | 95822.50 |
| Authors | Fedorov, E.,Manoilov, K.Y.,Verkhusha, V.,Almo, S.C.,Ghosh, A. (deposition date: 2021-07-06, release date: 2021-11-24, Last modification date: 2023-10-18) |
| Primary citation | Manoilov, K.Y.,Ghosh, A.,Almo, S.C.,Verkhusha, V.V. Structural and Functional Characterization of a Biliverdin-Binding Near-Infrared Fluorescent Protein From the Serpin Superfamily. J.Mol.Biol., 434:167359-167359, 2021 Cited by PubMed Abstract: Biliverdin-binding serpins (BBSs) are proteins that are responsible for coloration in amphibians and fluoresce in the near-infrared (NIR) spectral region. Here we produced the first functional recombinant BBS of the polka-dot treefrog Boana punctata (BpBBS), assembled with its biliverdin (BV) chromophore, and report its biochemical and photochemical characterization. We determined the crystal structure of BpBBS at 2.05 Å resolution, which demonstrated its structural homology to the mammalian protease inhibitor alpha-1-antitrypsin. BV interaction with BpBBS was studied and it was found that the N-terminal polypeptide (residues 19-50) plays a critical role in the BV binding. By comparing BpBBS with the available NIR fluorescent proteins and expressing it in mammalian cells, we demonstrated its potential as a NIR imaging probe. These results provide insight into the non-inhibitory function of serpins, provide a basis for improving their performance in mammalian cells, and suggest possible paths for the development of BBS-based fluorescent probes. PubMed: 34798132DOI: 10.1016/j.jmb.2021.167359 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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