4fwi | pdb_00004fwi

Crystal structure of the nucleotide-binding domain of a dipeptide ABC transporter

spinqualitylabelsall models 4fwi, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fwi is a 1 chain structure with sequence from Caldanaerobacter subterraneus subsp. tengcongensis MB4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.892Å Ligands: ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DPPD_CALS4 Part of the ABC transporter Dpp involved in dipeptide transport. Responsible for energy coupling to the transport system.[UniProtKB:A2RI77] Publication Abstract from PubMed Dipeptide permease (Dpp), which belongs to an ABC transport system, imports peptides consisting of two or three L-amino acids from the matrix to the cytoplasm in microbes. Previous studies have indicated that haem competes with dipeptides to bind DppA in vitro and in vivo and that the Dpp system can also translocate haem. Here, the crystal structure of DppD, the nucleotide-binding domain (NBD) of the ABC-type dipeptide/oligopeptide/nickel-transport system from Thermoanaerobacter tengcongensis, bound with ATP, Mg(2+) and a [4Fe-4S] iron-sulfur cluster is reported. The N-terminal domain of DppD shares a similar structural fold with the NBDs of other ABC transporters. Interestingly, the C-terminal domain of DppD contains a [4Fe-4S] cluster. The UV-visible absorbance spectrum of DppD was consistent with the presence of a [4Fe-4S] cluster. A search with DALI revealed that the [4Fe-4S] cluster-binding domain is a novel structural fold. Structural analysis and comparisons with other ABC transporters revealed that this iron-sulfur cluster may act as a mediator in substrate (dipeptide or haem) binding by electron transfer and may regulate the transport process in Dpp ABC transport systems. The crystal structure provides a basis for understanding the properties of ABC transporters and will be helpful in investigating the functions of NBDs in the regulation of ABC transporter activity. Structure of the nucleotide-binding domain of a dipeptide ABC transporter reveals a novel iron-sulfur cluster-binding domain.,Li X, Zhuo W, Yu J, Ge J, Gu J, Feng Y, Yang M, Wang L, Wang N Acta Crystallogr D Biol Crystallogr. 2013 Feb;69(Pt 2):256-65. doi:, 10.1107/S0907444912045180. Epub 2013 Jan 19. PMID:23385461 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

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