Database accession: MF7000495
Name: Glyoxalase (Gossypium hirsutum)
PDB ID: 7vq6
Experimental method: X-ray (1.39 Å)
Assembly: Homodimer
Source organism: Gossypium hirsutum
Primary publication of the structure:
Hu Y, Li H, Min J, Yu Y, Liu W, Huang JW, Zhang L, Yang Y, Dai L, Chen CC, Guo RT
Crystal structure and biochemical analysis of the specialized deoxynivalenol-detoxifying glyoxalase SPG from Gossypium hirsutum.
(2022) Int. J. Biol. Macromol. 200: 388-396
PMID: 35051496
Abstract:
Deoxynivalenol (DON) and its acetylated derivatives such as 3-acetyldeoxynivalenol (3A-DON) and 15-acetyldeoxynivalenol (15A-DON) are notorious mycotoxins in Fusarium contaminated cereals, which pose a great threat to human and livestock health. The specialized glyoxalase I from Gossypium hirsutum (SPG) can lower the toxicity of 3A-DON by conducting isomerization to transfer C8 carbonyl to C7 and double bond from C9-C10 to C8-C9. Here we report that the substrate-flexible SPG can also recognize 15A-DON and DON, probably following the same isomerization mechanism as that for 3A-DON. The crystallographic, mutagenesis, and biochemical analyses revealed that SPG provides a hydrophobic pocket to accommodate the substrate and residue E167 might serve as the catalytic base. A variant SPGY62A that was constructed based on structure-based protein engineering exhibited elevated catalytic activity towards DON, 3A-DON, and 15A-DON by >70%. Furthermore, variant SPGY62A was successfully expressed in Pichia pastoris, whose catalytic activity was also compared to that produced in Escherichia coli. These results provide a blueprint for further protein engineering of SPG and reveal the potential applications of the enzyme in detoxifying DON, 3A-DON and 15A-DON.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
lactoylglutathione lyase activity lactoylglutathione lyase activity
metal ion binding metal ion binding
Biological process: not assigned
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Lactoylglutathione lyase
Source organism: Gossypium hirsutum
Length: 181 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMGSMDSKESPANNPGLHTPPDEATKGYIMQQTMFRIKDPKRTLEFYSRVLGMSLLNKVDVPYMKMTLYMMGYEDVSSAPSDPVEKTIWTFGRPATMELTHFWGTENDPEFKGYHNGNSEPIGFGHIGITVDDMYKACERFESLGVEFVKKPSDGYTFIKDPDGYWIEIFDLNGIRAIVNTL
UniProtKB AC: A0A1U8Q028 (positions: 6-180)
Coverage: 96%
Name: Lactoylglutathione lyase
Source organism: Gossypium hirsutum
Length: 181 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMGSMDSKESPANNPGLHTPPDEATKGYIMQQTMFRIKDPKRTLEFYSRVLGMSLLNKVDVPYMKMTLYMMGYEDVSSAPSDPVEKTIWTFGRPATMELTHFWGTENDPEFKGYHNGNSEPIGFGHIGITVDDMYKACERFESLGVEFVKKPSDGYTFIKDPDGYWIEIFDLNGIRAIVNTL
UniProtKB AC: A0A1U8Q028 (positions: 6-180)
Coverage: 96%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Evidence level: Indirect evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
The VOC superfamily of metalloenzymes is characterized by a three-dimensional domain-swapped arrangement of tandem βαβββ-motifs (PMID:24447055). The original gene duplication event led to the βαβββ tandem structure, which appears to require dimerization for stability. Two different forms of domain-swapped dimers may coexist in solution (PMID:12121648) in which both subunits of the homodimer participate in coordination of each metal ion and formation of the U-shaped active sites in the enzyme (PMID:24004181). The complex is predominantly dimeric in solution (gel filtration) (PMID:12121648).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
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