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Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.

ABSTRACT: Glycosyltransferases (GTs) are responsible for transferring glycosyl moieties from activated sugar donors to certain acceptors, among which the GT1 family enzymes have been known for their outstanding glycosylation capacities toward diverse natural products, such as glycolipids, flavonoids and macrolides etc. However, there still lacks a systematic collation of this important family members. In this minireview, all the GT1 family sequences were phylogenetically analyzed, and the grouping of GT1 proteins exhibited a taxonomic life domain-dependent pattern, revealing many untapped clades of GTs. The further phylogenetic analysis of the characterized GTs facilitated the classification of substrates coverage of GT1 family enzymes from different life domains, whereby the GTs from bacteria can tolerate a wider spectrum of chemical skeletons as substrates, showing higher promiscuity than those from other domains. Furthermore, the sequence sizes of GTs from different domains were compared to understand their different substrates selectivity. Based on the multiple sequence alignments of 28 representative GT1 enzymes with crystal structures, two critical regions located in the N-terminal of GTs were identified, which were most variable among sequences from different taxonomic domains and essential for substrates binding and/or catalysis. The key roles of these two regions were validated by enumerating the influential residues that interacted with substrates in the representative structures from bacteria and plants. The atlas for GT1 family in terms of phylogeny, substrates selectivity, sequence length, and critical motifs provides the clues for the exploration of unknown GT1s and rational engineering of known enzymes, synthesizing novel promising glycoconjugates for pharmaceutical application.

SUBMITTER: Zhang P

PROVIDER: S-EPMC7316871 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.

Zhang Peng P Zhang Zheng Z Zhang Lijuan L Wang Jingjing J Wu Changsheng C Wu Changsheng C

Computational and structural biotechnology journal 20200610

Glycosyltransferases (GTs) are responsible for transferring glycosyl moieties from activated sugar donors to certain acceptors, among which the GT1 family enzymes have been known for their outstanding glycosylation capacities toward diverse natural products, such as glycolipids, flavonoids and macrolides <i>etc</i>. However, there still lacks a systematic collation of this important family members. In this minireview, all the GT1 family sequences were phylogenetically analyzed, and the grouping ...[more]

PMID: 32637037

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Project description:Neuronal and glial glutamate transporters remove the excitatory neurotransmitter glutamate from the synaptic cleft and thus prevent neurotoxicity. The proteins belong to a large and widespread family of secondary transporters, including bacterial glutamate, serine, and C4-dicarboxylate transporters; mammalian neutral-amino-acid transporters; and an increasing number of bacterial, archaeal, and eukaryotic proteins that have not yet been functionally characterized. Sixty members of the glutamate transporter family were found in the databases on the basis of sequence homology. The amino acid sequences of the carriers have diverged enormously. Homology between the members of the family is most apparent in a stretch of approximately 150 residues in the C-terminal part of the proteins. This region contains four reasonably well-conserved sequence motifs, all of which have been suggested to be part of the translocation pore or substrate binding site. Phylogenetic analysis of the C-terminal stretch revealed the presence of five subfamilies with characterized members: (i) the eukaryotic glutamate transporters, (ii) the bacterial glutamate transporters, (iii) the eukaryotic neutral-amino-acid transporters, (iv) the bacterial C4-dicarboxylate transporters, and (v) the bacterial serine transporters. A number of other subfamilies that do not contain characterized members have been defined. In contrast to their amino acid sequences, the hydropathy profiles of the members of the family are extremely well conserved. Analysis of the hydropathy profiles has suggested that the glutamate transporters have a global structure that is unique among secondary transporters. Experimentally, the unique structure of the transporters was recently confirmed by membrane topology studies. Although there is still controversy about part of the topology, the most likely model predicts the presence of eight membrane-spanning alpha-helices and a loop-pore structure which is unique among secondary transporters but may resemble loop-pores found in ion channels. A second distinctive structural feature is the presence of a highly amphipathic membrane-spanning helix that provides a hydrophilic path through the membrane. Recent data from analysis of site-directed mutants and studies on the mechanism and pharmacology of the transporters are discussed in relation to the structural model.

Dataset Information

Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.

Publications

Glycosyltransferase GT1 family: Phylogenetic distribution, substrates coverage, and representative structural features.

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