3gf3 | pdb_00003gf3

Glutaconyl-coA decarboxylase A subunit from Clostridium symbiosum co-crystallized with glutaconyl-coA

spinqualitylabelsall models 3gf3, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gf3 is a 1 chain structure with sequence from Clostridium symbiosum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: CL, COO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7TVP1_CLOSY Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Glutaconyl-CoA decarboxylase (Gcd) couples the biotin-dependent decarboxylation of glutaconyl-CoA with the generation of an electrochemical Na(+) gradient. Sequencing of the genes encoding all subunits of the Clostridium symbiosum decarboxylase membrane complex revealed that it comprises two distinct biotin carrier subunits, GcdC(1) and GcdC(2), which differ in the length of a central alanine- and proline-rich linker domain. Co-crystallization of the decarboxylase subunit GcdA with the substrate glutaconyl-CoA, the product crotonyl-CoA, and the substrate analogue glutaryl-CoA, respectively, resulted in a high resolution model for substrate binding and catalysis revealing remarkable structural changes upon substrate binding. Unlike the GcdA structure from Acidaminococcus fermentans, these data suggest that in intact Gcd complexes, GcdA is associated as a tetramer crisscrossed by a network of solvent-filled tunnels. An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases.,Kress D, Brugel D, Schall I, Linder D, Buckel W, Essen LO J Biol Chem. 2009 Oct 9;284(41):28401-9. Epub 2009 Aug 4. PMID:19654317 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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