5ERS
GephE in complex with Mg(2+) - AMP
Summary for 5ERS
| Entry DOI | 10.2210/pdb5ers/pdb |
| Descriptor | Gephyrin, ADENOSINE MONOPHOSPHATE, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | moco and wco biosynthesis, moco, amp with mg, transferase |
| Biological source | Rattus norvegicus (Norway Rat) |
| Cellular location | Cell junction, synapse : Q03555 |
| Total number of polymer chains | 1 |
| Total formula weight | 46650.55 |
| Authors | Kasaragod, V.B.,Schindelin, H. (deposition date: 2015-11-15, release date: 2016-05-04, Last modification date: 2024-01-10) |
| Primary citation | Kasaragod, V.B.,Schindelin, H. Structural Framework for Metal Incorporation during Molybdenum Cofactor Biosynthesis. Structure, 24:782-788, 2016 Cited by PubMed Abstract: The molybdenum cofactor (Moco) is essential for the catalytic activity of all molybdenum-containing enzymes with the exception of nitrogenase. Moco biosynthesis follows an evolutionarily highly conserved pathway and genetic deficiencies in the corresponding human enzymes result in Moco deficiency, which manifests itself in severe neurological symptoms and death in childhood. In humans the final steps of Moco biosynthesis are catalyzed by gephyrin, specifically the penultimate adenylation of molybdopterin (MPT) by its N-terminal G domain (GephG) and the final metal incorporation by its C-terminal E domain (GephE). To better understand the poorly defined molecular framework of this final step, we determined high-resolution crystal structures of GephE in the apo state and in complex with ADP, AMP, and molybdate. Our data provide novel insights into the catalytic steps leading to final Moco maturation, namely deadenylation as well as molybdate binding and insertion. PubMed: 27112598DOI: 10.1016/j.str.2016.02.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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