3GF3

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

Summary for 3GF3

• Entry DOI: 10.2210/pdb3gf3/pdb
• Related: 3GF7 3GLM 3GMA
• Descriptor: Glutaconyl-CoA decarboxylase subunit A, CROTONYL COENZYME A, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: glutaconyl-coa decarboxylase, sodium ion transport, biotin, glutamate fermentation, lyase
• Biological source: Clostridium symbiosum
• Total number of polymer chains: 1
• Total formula weight: 65895.04

Authors

Kress, D.,Brugel, D.,Buckel, W.,Essen, L.-O. (deposition date: 2009-02-26, release date: 2009-07-28, Last modification date: 2023-11-01)

Primary citation

Kress, D.,Brugel, D.,Schall, I.,Linder, D.,Buckel, W.,Essen, L.-O.
An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases
J.Biol.Chem., 284:28401-28409, 2009

PubMed Abstract: 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.

PubMed: 19654317
DOI: 10.1074/jbc.M109.037762

Experimental method

X-RAY DIFFRACTION (1.75 Å)