Structural highlights
4g1u is a 4 chain structure with sequence from "bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Gene: | hmuU, YPO0280, y0540, YP_0435 ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900), hmuV, YPO0279, y0539, YP_0434 ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[HMUU_YERPE] Part of the binding-protein-dependent transport system for hemin; probably responsible for the translocation of the substrate across the membrane. [HMUV_YERPE] Part of the ABC transporter complex HmuTUV involved in hemin import. Responsible for energy coupling to the transport system (Probable).[1]
Publication Abstract from PubMed
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 A 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.
X-ray structure of the Yersinia pestis heme transporter HmuUV.,Woo JS, Zeltina A, Goetz BA, Locher KP Nat Struct Mol Biol. 2012 Dec;19(12):1310-5. doi: 10.1038/nsmb.2417. Epub 2012, Nov 11. PMID:23142986[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thompson JM, Jones HA, Perry RD. Molecular characterization of the hemin uptake locus (hmu) from Yersinia pestis and analysis of hmu mutants for hemin and hemoprotein utilization. Infect Immun. 1999 Aug;67(8):3879-92. PMID:10417152
- ↑ Woo JS, Zeltina A, Goetz BA, Locher KP. X-ray structure of the Yersinia pestis heme transporter HmuUV. Nat Struct Mol Biol. 2012 Dec;19(12):1310-5. doi: 10.1038/nsmb.2417. Epub 2012, Nov 11. PMID:23142986 doi:http://dx.doi.org/10.1038/nsmb.2417
