6H9F
Structure of glutamate mutase reconstituted with bishomo-coenzyme B12
Summary for 6H9F
| Entry DOI | 10.2210/pdb6h9f/pdb |
| Descriptor | Glutamate mutase sigma subunit, Glutamate mutase epsilon subunit, COBALAMIN, ... (6 entities in total) |
| Functional Keywords | coenzyme b12, co-c-bond, radical reaction, tim-barrel, rossman-fold, isomerase |
| Biological source | Clostridium cochlearium More |
| Total number of polymer chains | 4 |
| Total formula weight | 140409.75 |
| Authors | Gruber, K.,Csitkovits, V.,Kratky, C. (deposition date: 2018-08-03, release date: 2019-08-14, Last modification date: 2024-01-31) |
| Primary citation | Gruber, K.,Csitkovits, V.,Lyskowski, A.,Kratky, C.,Krautler, B. Structure-Based Demystification of Radical Catalysis by a Coenzyme B 12 Dependent Enzyme-Crystallographic Study of Glutamate Mutase with Cofactor Homologues. Angew.Chem.Int.Ed.Engl., 61:e202208295-e202208295, 2022 Cited by PubMed Abstract: Catalysis by radical enzymes dependent on coenzyme B (AdoCbl) relies on the reactive primary 5'-deoxy-5'adenosyl radical, which originates from reversible Co-C bond homolysis of AdoCbl. This bond homolysis is accelerated roughly 10 -fold upon binding the enzyme substrate. The structural basis for this activation is still strikingly enigmatic. As revealed here, a displaced firm adenosine binding cavity in substrate-loaded glutamate mutase (GM) causes a structural misfit for intact AdoCbl that is relieved by the homolytic Co-C bond cleavage. Strategically interacting adjacent adenosine- and substrate-binding protein cavities provide a tight caged radical reaction space, controlling the entire radical path. The GM active site is perfectly structured for promoting radical catalysis, including "negative catalysis", a paradigm for AdoCbl-dependent mutases. PubMed: 35793207DOI: 10.1002/anie.202208295 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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