Publication: Computational characterizations of GDP-mannose 4,6-dehydratase (NoeL) Rhizobial proteins
Issued Date
2021-10-01
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14320983
01728083
01728083
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2-s2.0-85104253421
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Mahidol University
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SCOPUS
Bibliographic Citation
Current Genetics. Vol.67, No.5 (2021), 769-784
Suggested Citation
Supajit Sraphet, Bagher Javadi Computational characterizations of GDP-mannose 4,6-dehydratase (NoeL) Rhizobial proteins. Current Genetics. Vol.67, No.5 (2021), 769-784. doi:10.1007/s00294-021-01184-1 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/76020
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Computational characterizations of GDP-mannose 4,6-dehydratase (NoeL) Rhizobial proteins
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Abstract
A growing body of evidence suggests that Nod Factors molecules are the critical structural components in nitrogen fixation. These molecules have been implicated in plant–microbe signaling. Many enzymes involved in Nod factors biosynthesis; however, the enzymes that decorate (modify) nod factor main structure play a vital role. Here, the computational analysis of GDP-mannose 4,6-dehydratase (NoeL) proteins with great impact in modification of nod factor structure in four genomes of agriculturally important rhizobia (Bradyrhizobium, Mesorhizobium, Rhizobium, Sinorhizobium) presented. The NoeL number of amino acids was in the range of 147 (M5AMF5) to 372 (A0A023XWX0, Q89TZ1). The molecular weights were around 41 KDa. The results showed that the strain-specific purification strategy should apply as the pI of the sequences varied significantly (in the range of 5.59 to 9.12). The enzyme sequences and eight 3-dimensional structures predicted with homology modeling and machine learning representing the phylogenetic tree revealed the stability of enzymes in different conditions (Instability and Aliphatic index); however, this stability is also strain-specific. Disulphide bonds were observed in some species; however, the pattern was not detected in all members of the same species. Alpha helix was the dominant secondary structure predicted in all cytoplasmic NoeL. All models were homo-tetramer with acceptable sequence identity, GMEAN and coverage (60, − 1.80, 88, respectively). Additionally, Ramachandran maps showed that more than 94% of residues are in favored regions. We also highlight several key characterizations of NoeL from four rhizobia genomes annotation. These findings provide novel insights into the complexity and diversity of NoeL enzymes among important rhizobia and suggest considering a broader framework of biofilm for future research.