2CN4

The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand

Summary for 2CN4

• Entry DOI: 10.2210/pdb2cn4/pdb
• Related: 1B2V 1DK0 1DKH 1YBJ
• Descriptor: HEMOPHORE HASA, PROTOPORPHYRIN IX CONTAINING FE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: domain swapping, transport protein, heme, iron, dimeric form, metal-binding
• Biological source: SERRATIA MARCESCENS
• Cellular location: Secreted: Q54450
• Total number of polymer chains: 2
• Total formula weight: 36958.72

Authors

Czjzek, M.,Letoffe, S.,Wandersman, C.,Delepierre, M.,Lecroisey, A.,Izadi-Pruneyre, N. (deposition date: 2006-05-18, release date: 2006-05-26, Last modification date: 2023-12-13)

Primary citation

Czjzek, M.,Letoffe, S.,Wandersman, C.,Delepierre, M.,Lecroisey, A.,Izadi-Pruneyre, N.
The Crystal Structure of the Secreted Dimeric Form of the Hemophore Hasa Reveals a Domain Swapping with an Exchanged Heme Ligand
J.Mol.Biol., 365:1176-, 2007

PubMed Abstract: To satisfy their iron needs, several Gram-negative bacteria use a heme uptake system involving an extracellular heme-binding protein called hemophore. The function of the hemophore is to acquire free or hemoprotein-bound heme and to transfer it to HasR, its specific outer membrane receptor, by protein-protein interaction. The hemophore HasA secreted by Serratia marcescens, an opportunistic pathogen, was the first to be identified and is now very well characterized. HasA is a monomer that binds one b heme with strong affinity. The heme in HasA is highly exposed to solvent and coordinated by an unusual pair of ligands, a histidine and a tyrosine. Here, we report the identification, the characterization and the X-ray structure of a dimeric form of HasA from S. marcescens: DHasA. We show that both monomeric and dimeric forms are secreted in iron deficient conditions by S. marcescens. The crystal structure of DHasA reveals that it is a domain swapped dimer. The overall structure of each monomeric subunit of DHasA is very similar to that of HasA but formed by parts coming from the two different polypeptide chains, involving one of the heme ligands. Consequently DHasA binds two heme molecules by residues coming from both polypeptide chains. We show here that, while DHasA can bind two heme molecules, it is not able to deliver them to the receptor HasR. However, DHasA can efficiently transfer its heme to the monomeric form that, in turn, delivers it to HasR. We assume that DHasA can function as a heme reservoir in the hemophore system.

PubMed: 17113104
DOI: 10.1016/J.JMB.2006.10.063

Experimental method

X-RAY DIFFRACTION (2.3 Å)