6lu4

Crystal structure of the substrate binding protein from Microbacterium hydrocarbonoxydans complexed with propylparaben

spinqualitylabelsall models 6lu4, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6lu4 is a 1 chain structure with sequence from Dsm 16089. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 36M Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Microbacterium hydrocarbonoxydans was isolated, using hydrazide compounds as its sole carbon source. The key enzyme that metabolizes these compounds was identified as hydrazidase, and the operon containing the gene coding for the enzyme, was revealed by genome sequencing. The operon also contained genes coding for an ATP-binding cassette transporter (ABC transporter), which was expected to transport the hydrazide compounds. Substrate binding protein (SBP), a component subunit of the transporter, plays an important role in recognizing the correct substrates for transport. Therefore, to elucidate the mechanism of recognition of the unnatural hydrazide compounds, we determined the crystal structures of the SBP, obtained from M. hydrocarbonoxydans (Mh-SBP), complexed with and without the hydrazide compound, at 2.2 A and 1.75 A resolutions, respectively. The overall structures of Mh-SBP were similar to those of the SBP in oligopeptide transporters such as OppA. On comparison, the liganded and unliganded structures of Mh-SBP showed an open - close conformation change. Interestingly, the binding mode of the compound to Mh-SBP was almost identical to that of the compound to hydrazidase, suggesting that the ABC transporter served transporting these compounds. Furthermore, based on the hydrazide complex structure, paraben, the other putative substrate of the protein, was successfully used with Mh-SBP to obtain the paraben complex structure. Structural basis of substrate recognition by the substrate binding protein (SBP) of a hydrazide transporter, obtained from Microbacterium hydrocarbonoxydans.,Shimamura K, Akiyama T, Yokoyama K, Takenoya M, Ito S, Sasaki Y, Yajima S Biochem Biophys Res Commun. 2020 Mar 3. pii: S0006-291X(20)30435-6. doi:, 10.1016/j.bbrc.2020.02.146. PMID:32143826 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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