6a2u | pdb_00006a2u

Crystal structure of gamma-alpha subunit complex from Burkholderia cepacia FAD glucose dehydrogenase

spinqualitylabelsall models 6a2u, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a2u is a 4 chain structure with sequence from Burkholderia cepacia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Ligands: FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3KLY3_BURM1 Publication Abstract from PubMed The bacterial flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase complex derived from Burkholderia cepacia (BcGDH) is a representative molecule of direct electron transfer-type FAD-dependent dehydrogenase complexes. In this study, the X-ray structure of BcGDHgammaalpha, the catalytic subunit (alpha-subunit) of BcGDH complexed with a hitchhiker protein (gamma-subunit), was determined. The most prominent feature of this enzyme is the presence of the 3Fe-4S cluster, which is located at the surface of the catalytic subunit and functions in intramolecular and intermolecular electron transfer from FAD to the electron-transfer subunit. The structure of the complex revealed that these two molecules are connected through disulfide bonds and hydrophobic interactions, and that the formation of disulfide bonds is required to stabilize the catalytic subunit. The structure of the complex revealed the putative position of the electron-transfer subunit. A comparison of the structures of BcGDHgammaalpha and membrane-bound fumarate reductases suggested that the whole BcGDH complex, which also includes the membrane-bound beta-subunit containing three heme c moieties, may form a similar overall structure to fumarate reductases, thus accomplishing effective electron transfer. X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein.,Yoshida H, Kojima K, Shiota M, Yoshimatsu K, Yamazaki T, Ferri S, Tsugawa W, Kamitori S, Sode K Acta Crystallogr D Struct Biol. 2019 Sep 1;75(Pt 9):841-851. doi: , 10.1107/S2059798319010878. Epub 2019 Aug 28. PMID:31478907 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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