7RED

Holo Hemophilin from A. baumannii

Summary for 7RED

• Entry DOI: 10.2210/pdb7red/pdb
• Descriptor: Hemophilin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: heme binding, secreted, metal transport
• Biological source: Acinetobacter baumannii NIPH 201
• Total number of polymer chains: 1
• Total formula weight: 25744.57

Authors

Bateman, T.J.,Shah, M.,Moraes, T.F. (deposition date: 2021-07-12, release date: 2021-11-17, Last modification date: 2024-05-22)

Primary citation

Bateman, T.J.,Shah, M.,Ho, T.P.,Shin, H.E.,Pan, C.,Harris, G.,Fegan, J.E.,Islam, E.A.,Ahn, S.K.,Hooda, Y.,Gray-Owen, S.D.,Chen, W.,Moraes, T.F.
A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii.
Nat Commun, 12:6270-6270, 2021

PubMed Abstract: Nutrient acquisition systems are often crucial for pathogen growth and survival during infection, and represent attractive therapeutic targets. Here, we study the protein machinery required for heme uptake in the opportunistic pathogen Acinetobacter baumannii. We show that the hemO locus, which includes a gene encoding the heme-degrading enzyme, is required for high-affinity heme acquisition from hemoglobin and serum albumin. The hemO locus includes a gene coding for a heme scavenger (HphA), which is secreted by a Slam protein. Furthermore, heme uptake is dependent on a TonB-dependent receptor (HphR), which is important for survival and/or dissemination into the vasculature in a mouse model of pulmonary infection. Our results indicate that A. baumannii uses a two-component receptor system for the acquisition of heme from host heme reservoirs.

PubMed: 34725337
DOI: 10.1038/s41467-021-26545-9

Experimental method

X-RAY DIFFRACTION (1.53 Å)