Multiplicity of carbohydrate-binding sites in β-prism fold lectins: occurrence and possible evolutionary implications

Sharma, Alok; Chandran, Divya; Singh, DD; Vijayan, M.

doi:10.1007/s12038-007-0111-3

Cited by 32 publications

(20 citation statements)

References 61 publications

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“…BP1 proteins also bind carbohydrates with up to three binding sites, and a common origin of BP1 and BP2 has been discussed without clear conclusion [42]. The large distance between BP1 and BP2 proteins in our cluster map (Fig.…”

Section: Resultsmentioning

confidence: 81%

β-Propeller Blades as Ancestral Peptides in Protein Evolution

Kopec

Lupas

2013

PLoS ONE

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Proteins of the β-propeller fold are ubiquitous in nature and widely used as structural scaffolds for ligand binding and enzymatic activity. This fold comprises between four and twelve four-stranded β-meanders, the so called blades that are arranged circularly around a central funnel-shaped pore. Despite the large size range of β-propellers, their blades frequently show sequence similarity indicative of a common ancestry and it has been proposed that the majority of β-propellers arose divergently by amplification and diversification of an ancestral blade. Given the structural versatility of β-propellers and the hypothesis that the first folded proteins evolved from a simpler set of peptides, we investigated whether this blade may have given rise to other folds as well. Using sequence comparisons, we identified proteins of four other folds as potential homologs of β-propellers: the luminal domain of inositol-requiring enzyme 1 (IRE1-LD), type II β-prisms, β-pinwheels, and WW domains. Because, with increasing evolutionary distance and decreasing sequence length, the statistical significance of sequence comparisons becomes progressively harder to distinguish from the background of convergent similarities, we complemented our analyses with a new method that evaluates possible homology based on the correlation between sequence and structure similarity. Our results indicate a homologous relationship of IRE1-LD and type II β-prisms with β-propellers, and an analogous one for β-pinwheels and WW domains. Whereas IRE1-LD most likely originated by fold-changing mutations from a fully formed PQQ motif β-propeller, type II β-prisms originated by amplification and differentiation of a single blade, possibly also of the PQQ type. We conclude that both β-propellers and type II β-prisms arose by independent amplification of a blade-sized fragment, which represents a remnant of an ancient peptide world.

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Section: Resultsmentioning

confidence: 81%

β-Propeller Blades as Ancestral Peptides in Protein Evolution

Kopec

Lupas

2013

PLoS ONE

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“…However, only one of the keys has a binding site in the archeal lectin domains, as in the case of artocarpin. It has been suggested in the case of β‐prism fold lectins also that the fold could have resulted from successive gene duplication, fusion and divergent evolution of a primitive Greek key based carbohydrate binding motif . It has been further suggested that there is a correlation between the average sequence identity among the three Greek keys and the number of binding sites.…”

Section: Resultsmentioning

confidence: 99%

Archeal lectins: An identification through a genomic search

2015

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Forty-six lectin domains which have homologues among well established eukaryotic and bacterial lectins of known three-dimensional structure, have been identified through a search of 165 archeal genomes using a multipronged approach involving domain recognition, sequence search and analysis of binding sites. Twenty-one of them have the 7-bladed β-propeller lectin fold while 16 have the β-trefoil fold and 7 the legume lectin fold. The remainder assumes the C-type lectin, the β-prism I and the tachylectin folds. Acceptable models of almost all of them could be generated using the appropriate lectins of known three-dimensional structure as templates, with binding sites at one or more expected locations. The work represents the first comprehensive bioinformatic study of archeal lectins. The presence of lectins with the same fold in all domains of life indicates their ancient origin well before the divergence of the three branches. Further work is necessary to identify archeal lectins which have no homologues among eukaryotic and bacterial species.

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“…The dual preference of VCC for complex N-linked glycans (25) and for O-linked sugars in asialofetuin might be a reflection of the multiple carbohydrate-binding specificities exhibited by ␤-prism fold lectins (34,35).…”

Section: C-terminal ␤-Prism Lectin Fold and Binding To Asialofetuin-mentioning

confidence: 99%

The β-Prism Lectin Domain of Vibrio cholerae Hemolysin Promotes Self-assembly of the β-Pore-forming Toxin by a Carbohydrate-independent Mechanism

Ganguly¹,

Mukherjee²,

Mazumdar³

et al. 2014

Journal of Biological Chemistry

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Background:Vibrio cholerae hemolysin is a pore-forming toxin with a ␤-prism lectin domain. Results: Although amphipathicity-driven interactions with lipids dominate membrane targeting, relocation of the lectin domain during toxin assembly generates entropy to push oligomerization and thereby promote pore formation. Conclusion:The lectin domain promotes toxin assembly by a carbohydrate-independent mechanism. Significance: A novel role for the lectin domain in protein oligomerization is revealed.

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Multiplicity of carbohydrate-binding sites in β-prism fold lectins: occurrence and possible evolutionary implications

Cited by 32 publications

References 61 publications

β-Propeller Blades as Ancestral Peptides in Protein Evolution

β-Propeller Blades as Ancestral Peptides in Protein Evolution

Archeal lectins: An identification through a genomic search

The β-Prism Lectin Domain of Vibrio cholerae Hemolysin Promotes Self-assembly of the β-Pore-forming Toxin by a Carbohydrate-independent Mechanism

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