8KI0

Crystal structure of the hemophore HasA from Pseudomonas protegens Pf-5 capturing Fe-tetraphenylporphyrin

Summary for 8KI0

• Entry DOI: 10.2210/pdb8ki0/pdb
• Descriptor: Heme acquisition protein HasAp, [5,10,15,20-tetraphenylporphyrinato(2-)-kappa~4~N~21~,N~22~,N~23~,N~24~]iron, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, ... (6 entities in total)
• Functional Keywords: heme acquisition protein, transport protein
• Biological source: Pseudomonas protegens Pf-5
• Total number of polymer chains: 2
• Total formula weight: 40165.33

Authors

Shisaka, Y.,Inaba, H.,Sugimoto, H.,Shoji, O. (deposition date: 2023-08-22, release date: 2024-03-27, Last modification date: 2024-05-15)

Primary citation

Inaba, H.,Shisaka, Y.,Ariyasu, S.,Sakakibara, E.,Ueda, G.,Aiba, Y.,Shimizu, N.,Sugimoto, H.,Shoji, O.
Heme-substituted protein assembly bridged by synthetic porphyrin: achieving controlled configuration while maintaining rotational freedom.
Rsc Adv, 14:8829-8836, 2024

PubMed Abstract: The use of biological host-guest interactions, specifically the binding of hemoprotein to heme, has attracted significant research interest in the design of artificial protein assemblies. However, because of the inherent flexibility of the propionic acid group of heme, it is difficult to control the positioning and orientation of the protein unit and to construct well-ordered structures. Herein, we report a heme-substituted protein dimer composed of the native hemoprotein HasA, which accommodates a tetraphenylporphyrin bearing an additional metal coordination site. The specific binding of the tetraphenylporphyrin with an additional metal coordination site that protrudes in a fixed direction confines the configuration of the dimer structure to a defined bent form. The small-angle X-ray scattering profile shows the dimer structure with a bent form and suggests dynamic rotational behavior while keeping its bent-core structure, resembling a bevel gear. This unique dimer structure demonstrates that the design of heme-substituted protein assemblies can be expanded to protein assemblies while maintaining the rotational freedom of the individual protein units.

PubMed: 38495978
DOI: 10.1039/d4ra01042f

Experimental method

X-RAY DIFFRACTION (1.45 Å)