7EMS
Crystal Structure of the HasAp L85A Mutant Capturing Iron Tetraphenylporphyrin
Summary for 7EMS
| Entry DOI | 10.2210/pdb7ems/pdb |
| Descriptor | Heme acquisition protein HasAp, [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | heme acquisition protein, transport protein |
| Biological source | Pseudomonas aeruginosa str. PAO1 |
| Total number of polymer chains | 3 |
| Total formula weight | 58987.40 |
| Authors | Shisaka, Y.,Sugimoto, H.,Shoji, O. (deposition date: 2021-04-14, release date: 2022-04-20, Last modification date: 2023-11-29) |
| Primary citation | Shisaka, Y.,Sakakibara, E.,Suzuki, K.,Stanfield, J.K.,Onoda, H.,Ueda, G.,Hatano, M.,Sugimoto, H.,Shoji, O. Tetraphenylporphyrin Enters the Ring: First Example of a Complex between Highly Bulky Porphyrins and a Protein. Chembiochem, 23:e202200095-e202200095, 2022 Cited by PubMed Abstract: Tetraphenylporphyrin (TPP) is a symmetrically substituted synthetic porphyrin whose properties can be readily modified, providing it with significant advantages over naturally occurring porphyrins. Herein, we report the first example of a stable complex between a native biomolecule, the haemoprotein HasA, and TPP as well as its derivatives. The X-ray crystal structures of nine different HasA-TPP complexes were solved at high resolutions. HasA capturing TPP derivatives was also demonstrated to inhibit growth of the opportunistic pathogen Pseudomonas aeruginosa. Mutant variants of HasA binding FeTPP were shown to possess a different mode of coordination, permitting the cyclopropanation of styrene. PubMed: 35352458DOI: 10.1002/cbic.202200095 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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