Structural highlights
8bql is a 2 chain structure with sequence from Desulfovibrio vulgaris str. Hildenborough. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Method: | X-ray diffraction, Resolution 1.906Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q72EJ1_DESVH
Publication Abstract from PubMed
Metal-dependent formate dehydrogenases (Fdh) catalyze the reversible conversion of CO(2) to formate, with unrivalled efficiency and selectivity. However, the key catalytic aspects of these enzymes remain unknown, preventing us from fully benefiting from their capabilities in terms of biotechnological applications. Here, we report a time-resolved characterization by X-ray crystallography of the Desulfovibrio vulgaris Hildenborough SeCys/W-Fdh during formate oxidation. The results allowed us to model five different intermediate structures and to chronologically map the changes occurring during enzyme reduction. Formate molecules were assigned for the first time to populate the catalytic pocket of a Fdh. Finally, the redox reversibility of DvFdhAB in crystals was confirmed by reduction and reoxidation structural studies.
Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation.,Vilela-Alves G, Manuel RR, Oliveira AR, Pereira IC, Romao MJ, Mota C Int J Mol Sci. 2022 Dec 28;24(1):476. doi: 10.3390/ijms24010476. PMID:36613918[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vilela-Alves G, Manuel RR, Oliveira AR, Pereira IC, Romao MJ, Mota C. Tracking W-Formate Dehydrogenase Structural Changes During Catalysis and Enzyme Reoxidation. Int J Mol Sci. 2022 Dec 28;24(1):476. doi: 10.3390/ijms24010476. PMID:36613918 doi:http://dx.doi.org/10.3390/ijms24010476
