8THE
Cryo-EM structure of Pseudomonas aeruginosa TonB-dependent transporter PhuR in complex with synthetic antibody and heme
This is a non-PDB format compatible entry.
Summary for 8THE
| Entry DOI | 10.2210/pdb8the/pdb |
| EMDB information | 41255 |
| Descriptor | Heme/hemoglobin uptake outer membrane receptor PhuR, Synthetic Antibody Heavy Chain, Synthetic Antibody Light Chain, ... (6 entities in total) |
| Functional Keywords | beta barrel, outer membrane protein, heme binding protein, heme transport, membrane protein |
| Biological source | Pseudomonas aeruginosa More |
| Total number of polymer chains | 3 |
| Total formula weight | 137743.51 |
| Authors | Knejski, P.,Erramilli, S.K.,Kossiakoff, A.A. (deposition date: 2023-07-15, release date: 2024-01-31, Last modification date: 2024-11-13) |
| Primary citation | Knejski, P.P.,Erramilli, S.K.,Kossiakoff, A.A. Chaperone-assisted cryo-EM structure of P. aeruginosa PhuR reveals molecular basis for heme binding. Structure, 32:411-, 2024 Cited by PubMed Abstract: Pathogenic bacteria, such as Pseudomonas aeruginosa, depend on scavenging heme for the acquisition of iron, an essential nutrient. The TonB-dependent transporter (TBDT) PhuR is the major heme uptake protein in P. aeruginosa clinical isolates. However, a comprehensive understanding of heme recognition and TBDT transport mechanisms, especially PhuR, remains limited. In this study, we employed single-particle cryogenic electron microscopy (cryo-EM) and a phage display-generated synthetic antibody (sAB) as a fiducial marker to enable the determination of a high-resolution (2.5 Å) structure of PhuR with a bound heme. Notably, the structure reveals iron coordination by Y529 on a conserved extracellular loop, shedding light on the role of tyrosine in heme binding. Biochemical assays and negative-stain EM demonstrated that the sAB specifically targets the heme-bound state of PhuR. These findings provide insights into PhuR's heme binding and offer a template for developing conformation-specific sABs against outer membrane proteins (OMPs) for structure-function investigations. PubMed: 38325368DOI: 10.1016/j.str.2024.01.007 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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