6ZXX
Catabolic reductive dehalogenase NpRdhA, N-terminally tagged.
Summary for 6ZXX
| Entry DOI | 10.2210/pdb6zxx/pdb |
| Descriptor | Oxidoreductase, NAD-binding/iron-sulfur cluster-binding protein, IRON/SULFUR CLUSTER, COBALAMIN, ... (8 entities in total) |
| Functional Keywords | reductive dehalogenase, b12, iron-sulfur, oxidoreductase |
| Biological source | Nitratireductor pacificus pht-3B |
| Total number of polymer chains | 3 |
| Total formula weight | 247116.09 |
| Authors | Leys, D.,Halliwell, T. (deposition date: 2020-07-30, release date: 2020-09-16, Last modification date: 2024-01-31) |
| Primary citation | Halliwell, T.,Fisher, K.,Payne, K.A.P.,Rigby, S.E.J.,Leys, D. Catabolic Reductive Dehalogenase Substrate Complex Structures Underpin Rational Repurposing of Substrate Scope. Microorganisms, 8:-, 2020 Cited by PubMed Abstract: Reductive dehalogenases are responsible for the reductive cleavage of carbon-halogen bonds during organohalide respiration. A variety of mechanisms have been proposed for these cobalamin and [4Fe-4S] containing enzymes, including organocobalt, radical, or cobalt-halide adduct based catalysis. The latter was proposed for the oxygen-tolerant cataboli reductive dehalogenase (NpRdhA). Here, we present the first substrate bound NpRdhA crystal structures, confirming a direct cobalt-halogen interaction is established and providing a rationale for substrate preference. Product formation is observed due to X-ray photoreduction. Protein engineering enables rational alteration of substrate preference, providing a future blue print for the application of this and related enzymes in bioremediation. PubMed: 32887524DOI: 10.3390/microorganisms8091344 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.99 Å) |
Structure validation
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