5XKB
Crystal Structure of HasAp with Fe-5,15-bisethynyl-10,20-diphenylporphyrin
Summary for 5XKB
Entry DOI | 10.2210/pdb5xkb/pdb |
Descriptor | Heme acquisition protein HasAp, 5,15-Bisethynyl-10,20-diphenylporphyrin containing FE (3 entities in total) |
Functional Keywords | heme acquisition protein, transport protein |
Biological source | Pseudomonas aeruginosa str. PAO1 |
Total number of polymer chains | 2 |
Total formula weight | 38931.90 |
Authors | Shoji, O.,Uehara, H.,Sugimoto, H.,Shiro, Y.,Watanabe, Y. (deposition date: 2017-05-06, release date: 2017-12-06, Last modification date: 2024-03-27) |
Primary citation | Uehara, H.,Shisaka, Y.,Nishimura, T.,Sugimoto, H.,Shiro, Y.,Miyake, Y.,Shinokubo, H.,Watanabe, Y.,Shoji, O. Structures of the Heme Acquisition Protein HasA with Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group Angew. Chem. Int. Ed. Engl., 56:15279-15283, 2017 Cited by PubMed Abstract: Iron(III)-5,15-diphenylporphyrin and several derivatives were accommodated by HasA, a heme acquisition protein secreted by Pseudomonas aeruginosa, despite possessing bulky substituents at the meso position of the porphyrin. Crystal structure analysis revealed that the two phenyl groups at the meso positions of porphyrin extend outside HasA. It was shown that the growth of P. aeruginosa was inhibited in the presence of HasA coordinating the synthetic porphyrins under iron-limiting conditions, and that the structure of the synthetic porphyrins greatly affects the inhibition efficiency. PubMed: 28921809DOI: 10.1002/anie.201707212 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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