5XA4

Crystal Structure of HasAp with Fe-5,15-Diazaporphyrin

Summary for 5XA4

• Entry DOI: 10.2210/pdb5xa4/pdb
• Descriptor: Heme acquisition protein HasAp, 10,20-Diphenyl-5,15-diaza-porphyrin 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: 38839.77

Authors

Shoji, O.,Uehara, H.,Sugimoto, H.,Shiro, Y.,Watanabe, Y. (deposition date: 2017-03-10, release date: 2017-12-06, Last modification date: 2023-11-22)

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

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: 28921809
DOI: 10.1002/anie.201707212

Experimental method

X-RAY DIFFRACTION (1.3 Å)