Crystal structure of a S-adenosyl-L-methionine-dependent O-methyltransferase-like enzyme from Aspergillus flavus.
Amino Acid Sequence
Aspergillus flavus
/ chemistry
Catalytic Domain
Crystallography, X-Ray
Evolution, Molecular
Fungal Proteins
/ chemistry
Gene Expression
Hydrogen Bonding
Methyltransferases
/ chemistry
Models, Molecular
Phylogeny
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Recombinant Proteins
/ chemistry
S-Adenosylhomocysteine
/ chemistry
S-Adenosylmethionine
/ chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Structure-Activity Relationship
Substrate Specificity
SAM-dependent methyltransferase
crystal structure
evolution
pericyclic reaction
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
received:
11
12
2019
revised:
05
08
2020
accepted:
25
08
2020
pubmed:
3
9
2020
medline:
25
5
2021
entrez:
3
9
2020
Statut:
ppublish
Résumé
S-adenosyl-L-methionine (SAM)-dependent methyltransferases (MTases) are widely distributed among almost all organisms and often characterized with conserved Rossmann fold, TIM barrel, and D×G×G×G motif. However, some MTases show no methyltransferase activity. In the present study, the crystal structure of LepI, one MTase-like enzyme isolated from A. flavus that catalyzes pericyclic reactions, was investigated to determine its structure-function relationship. The overall structure of LepI in complex with the SAM mimic S-adenosyl-L-homocysteine (SAH) (PDB ID: 6IV7) indicated that LepI is a tetramer in solution. The residues His133, Arg197, Arg295, and Asp296 located near the active site can form hydrogen bonds with the substrate, thus participating in catalytic reactions. The binding of SAH in LepI is almost identical to that in other resolved MTases; however, the location of catalytic residues differs significantly. Phylogenetic trials suggest that LepI proteins share a common ancestor in plants and algae, which may explain the conserved SAM-binding site. However, the accelerated evolution of A. flavus has introduced both functional and structural changes in LepI. More importantly, the residue Arg295, which is unique to LepI, might be a key determinant for the altered enzymatic behavior. Collectively, the differences in the composition of catalytic residues, as well as the unique tetrameric form of LepI, define its unique enzymatic behavior. The present work provides an additional understanding of the structure-function relationship of MTases and MTase-like enzymes.
Substances chimiques
Fungal Proteins
0
Recombinant Proteins
0
S-Adenosylmethionine
7LP2MPO46S
S-Adenosylhomocysteine
979-92-0
Methyltransferases
EC 2.1.1.-
methionine S-methyltransferase
EC 2.1.1.12
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
185-192Informations de copyright
© 2020 Wiley Periodicals LLC.
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