7A76
Bacillithiol Disulfide Reductase Bdr (YpdA) from Bacillus cereus
Summary for 7A76
| Entry DOI | 10.2210/pdb7a76/pdb |
| Related | 7A7B 7APR |
| Descriptor | THIOREDOXIN REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | disulfide reductase, fad, flavoprotein, nadph, oxidoreductase |
| Biological source | Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711) |
| Total number of polymer chains | 4 |
| Total formula weight | 149335.44 |
| Authors | Hammerstad, M.,Gudim, I.,Hersleth, H.-P. (deposition date: 2020-08-27, release date: 2020-12-30, Last modification date: 2024-05-01) |
| Primary citation | Hammerstad, M.,Gudim, I.,Hersleth, H.P. The Crystal Structures of Bacillithiol Disulfide Reductase Bdr (YpdA) Provide Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductase. Biochemistry, 59:4793-4798, 2020 Cited by PubMed Abstract: Low G+C Gram-positive Firmicutes, such as the clinically important pathogens and , use the low-molecular weight thiol bacillithiol (BSH) as a defense mechanism to buffer the intracellular redox environment and counteract oxidative stress encountered by human neutrophils during infections. The protein YpdA has recently been shown to function as an essential NADPH-dependent reductase of oxidized bacillithiol disulfide (BSSB) resulting from stress responses and is crucial for maintaining the reduced pool of BSH and cellular redox balance. In this work, we present the first crystallographic structures of YpdAs, namely, those from and . Our analyses reveal a uniquely organized biological tetramer; however, the structure of the monomeric subunit is highly similar to those of other flavoprotein disulfide reductases. The absence of a redox active cysteine in the vicinity of the FAD isoalloxazine ring implies a new direct disulfide reduction mechanism, which is backed by the presence of a potentially gated channel, serving as a putative binding site for BSSB in the proximity of the FAD cofactor. We also report enzymatic activities for both YpdAs, which along with the structures presented in this work provide important structural and functional insight into a new class of FAD-containing NADPH-dependent oxidoreductases, related to the emerging fight against pathogenic bacteria. PubMed: 33326741DOI: 10.1021/acs.biochem.0c00745 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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