4G1U
X-ray structure of the bacterial heme transporter HmuUV from Yersinia pestis
Summary for 4G1U
| Entry DOI | 10.2210/pdb4g1u/pdb |
| Descriptor | Hemin transport system permease protein hmuU, Hemin import ATP-binding protein HmuV, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | membrane transporter, type ii abc importer, hmut, plasma membrane, transport protein-hydrolase complex, transport protein/hydrolase |
| Biological source | Yersinia pestis More |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: Q56992 Cell inner membrane; Peripheral membrane protein (By similarity): Q56993 |
| Total number of polymer chains | 4 |
| Total formula weight | 136278.83 |
| Authors | Woo, J.-S.,Goetz, B.A.,Zeltina, A.,Locher, K.P. (deposition date: 2012-07-11, release date: 2012-12-19, Last modification date: 2024-03-20) |
| Primary citation | Woo, J.-S.,Zeltina, A.,Goetz, B.A.,Locher, K.P. X-ray structure of the Yersinia pestis heme transporter HmuUV. Nat.Struct.Mol.Biol., 19:1310-1315, 2012 Cited by PubMed Abstract: HmuUV is a bacterial ATP-binding cassette (ABC) transporter that catalyzes heme uptake into the cytoplasm of the gram-negative pathogen Yersinia pestis. We report the crystal structure of HmuUV at 3.0 Å resolution in a nucleotide-free state, which features a heme translocation pathway in an outward-facing conformation, poised to accept a heme from the cognate periplasmic binding protein HmuT. A new assay allowed us to determine in vitro rates of HmuUV-catalyzed heme transport into proteoliposomes and to establish the role of conserved residues in the translocation pathway of HmuUV and at the interface with HmuT. Differences in architecture relative to the related vitamin B(12) transporter BtuCD suggest an adaptation of HmuUV for its smaller substrate. Our study also suggests that type II ABC importers, which include bacterial iron-siderophore, heme and cobalamin transporters, have a coupling mechanism distinct from that of other ABC transporters. PubMed: 23142986DOI: 10.1038/nsmb.2417 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.008 Å) |
Structure validation
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