6y16

CRYSTAL STRUCTURE OF TMARGBP DOMAIN 1 IN COMPLEX WITH THE GUANIDINIUM ION

spinqualitylabelsall models 6y16, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6y16 is a 2 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: EDO, GAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9WZ62_THEMA Publication Abstract from PubMed Thermotoga maritima Arginine Binding Protein has been extensively characterized because of its peculiar features and its possible use as a biosensor. In this characterization, deletion of the C-terminal helix to obtain the monomeric protein TmArgBP(20-233) and dissection of the monomer in its two domains, D1 and D2, have been performed. In the present study the stability of these three forms against guanidinium chloride is investigated by means of circular dichroism and differential scanning calorimetry measurements. All three proteins show a high conformational stability; moreover, D1 shows an unusual behavior in the presence of low concentrations of guanidinium chloride. This finding has led us to investigate a possible binding interaction by means of isothermal titration calorimetry and X-ray crystallography; the results indicate that D1 is able to bind the guanidinium ion (GuH(+)), due to its similarity with the arginine terminal moiety. The analysis of the structural and dynamic properties of the D1-GuH(+) complex indicates that the protein binds the ligand through multiple and diversified interactions. An exhaustive survey of the binding modes of GuH(+) to proteins indicates that this is a rather common feature. These observations provide interesting insights into the effects that GuH(+) is able to induce in protein structures. Guanidinium binding to proteins: The intriguing effects on the D1 and D2 domains of Thermotoga maritima Arginine Binding Protein and a comprehensive analysis of the Protein Data Bank.,Cozzolino S, Balasco N, Vigorita M, Ruggiero A, Smaldone G, Del Vecchio P, Vitagliano L, Graziano G Int J Biol Macromol. 2020 Jul 4;163:375-385. doi: 10.1016/j.ijbiomac.2020.06.290. PMID:32629051 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

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