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8Q0C

Human carbonic anhydrase II containing 3-fluorotyrosine

Summary for 8Q0C
Entry DOI10.2210/pdb8q0c/pdb
Related8B29 8P6U 8PHL
DescriptorCarbonic anhydrase 2, ZINC ION, MERCURIBENZOIC ACID, ... (4 entities in total)
Functional Keywordshuman carbonic anhydrase ii, hcaii, 5-fluorotryptophane, in-cell nmr, lyase
Biological sourceHomo sapiens (human)
Total number of polymer chains1
Total formula weight29601.82
Authors
Pham, L.B.T.,Costantino, A.,Barbieri, L.,Calderone, V.,Luchinat, E.,Banci, L. (deposition date: 2023-07-28, release date: 2024-03-06, Last modification date: 2024-11-13)
Primary citationCostantino, A.,Pham, L.B.T.,Barbieri, L.,Calderone, V.,Ben-Nissan, G.,Sharon, M.,Banci, L.,Luchinat, E.
Controlling the incorporation of fluorinated amino acids in human cells and its structural impact.
Protein Sci., 33:e4910-e4910, 2024
Cited by
PubMed Abstract: Fluorinated aromatic amino acids (FAAs) are promising tools when studying protein structure and dynamics by NMR spectroscopy. The incorporation FAAs in mammalian expression systems has been introduced only recently. Here, we investigate the effects of FAAs incorporation in proteins expressed in human cells, focusing on the probability of incorporation and its consequences on the F NMR spectra. By combining F NMR, direct MS and x-ray crystallography, we demonstrate that the probability of FAA incorporation is only a function of the FAA concentration in the expression medium and is a pure stochastic phenomenon. In contrast with the MS data, the x-ray structures of carbonic anhydrase II reveal that while the 3D structure is not affected, certain positions lack fluorine, suggesting that crystallization selectively excludes protein molecules featuring subtle conformational modifications. This study offers a predictive model of the FAA incorporation efficiency and provides a framework for controlling protein fluorination in mammalian expression systems.
PubMed: 38358125
DOI: 10.1002/pro.4910
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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