Crystallization and biochemical characterization of an archaeal lectin from<i>Methanococcus voltae</i>A3

Sivaji, N.; Abhinav, K.V.; Vijayan, M.

doi:10.1107/s2053230x17006173

Cited by 4 publications

(2 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A preliminary hemagglutination assay of TTHA1873 was performed according to the protocol described in Sivaji et al (2017). Using the serial dilution method, the hemagglutination assay of TTHA1873 was performed in a U-bottom 96-well plate.…”

Section: Preliminary Hemagglutination Assaymentioning

confidence: 99%

Structure of the hypothetical protein TTHA1873 from Thermus thermophilus

Yuvaraj

Chaudhary

Jeyakanthan

et al. 2022

Acta Crystallogr F Struct Biol Commun

View full text Add to dashboard Cite

The crystal structure of an uncharacterized hypothetical protein, TTHA1873 from Thermus thermophilus, has been determined by X-ray crystallography to a resolution of 1.78 Å using the single-wavelength anomalous dispersion method. The protein crystallized as a dimer in two space groups: P43212 and P6122. Structural analysis of the hypothetical protein revealed that the overall fold of TTHA1873 has a β-sandwich jelly-roll topology with nine β-strands. TTHA1873 is a dimeric metal-binding protein that binds to two Ca2+ ions per chain, with one on the surface and the other stabilizing the dimeric interface of the two chains. A structural homology search indicates that the protein has moderate structural similarity to one domain of cell-surface proteins or agglutinin receptor proteins. Red blood cells showed visible agglutination at high concentrations of the hypothetical protein.

show abstract

Section: Preliminary Hemagglutination Assaymentioning

confidence: 99%

Structure of the hypothetical protein TTHA1873 from Thermus thermophilus

Yuvaraj

Chaudhary

Jeyakanthan

et al. 2022

Acta Crystallogr F Struct Biol Commun

View full text Add to dashboard Cite

show abstract

“…Lectins are a large group of proteins that specifically and reversibly bind carbohydrates [35]. They are ubiquitously found in nature, including bacteria, animals, plants, viruses, fungi and archaea [36][37][38]. In their host organisms, they are involved in diverse biological processes, such as adhesion, cell development and apoptosis, signalling and trafficking among others [35,36,39].…”

Section: Introductionmentioning

confidence: 99%

‘Clickable lectins’: bioorthogonal reactive handles facilitate the directed conjugation of lectins in a modular fashion

et al. 2019

View full text Add to dashboard Cite

show abstract

Structural and related studies on Mevo lectin from Methanococcus voltae A3: the first thorough characterization of an archeal lectin and its interactions

et al. 2020

View full text Add to dashboard Cite

Abstract Crystallographic and solution studies of Mevo lectin and its complexes, the first effort of its kind on an archeal lectin, reveal a structure similar to β-prism I fold lectins from plant and animal sources, but with a quaternary association involving a ring structure with seven-fold symmetry. Each subunit in the heptamer carries one sugar binding site on the first Greek key motif. The oligomeric interface is primarily made up of a parallel β-sheet involving a strand of Greek key Ι of one subunit and Greek key ΙΙΙ from a neighbouring subunit. The crystal structures of the complexes of the lectin with mannose, αMan(1,2)αMan, αMan(1,3)αMan, a mannotriose and a mannopentose revealed a primary binding site similar to that found in other mannose specific β-prism I fold lectins. The complex with αMan(1,3)αMan provides an interesting case in which a few subunits have the reducing end at the primary binding site, while the majority have the non-reducing end at the primary binding site. The structures of complexes involving the trisaccharide and the pentasaccharide exhibit cross-linking among heptameric molecules. The observed arrangements maybe relevant to the multivalency of the lectin. Phylogenetic analysis of amino acid sequences indicates that Mevo lectin is closer to β-prism I fold animal lectins than with those of plant origin. The results presented here reinforce the conclusion regarding the existence of lectins in all three domains of life. It would also appear that lectins evolved to the present form before the three domains diverged.

show abstract

Crystallization and biochemical characterization of an archaeal lectin fromMethanococcus voltaeA3

Cited by 4 publications

References 35 publications

Structure of the hypothetical protein TTHA1873 from Thermus thermophilus

Structure of the hypothetical protein TTHA1873 from Thermus thermophilus

‘Clickable lectins’: bioorthogonal reactive handles facilitate the directed conjugation of lectins in a modular fashion

Structural and related studies on Mevo lectin from Methanococcus voltae A3: the first thorough characterization of an archeal lectin and its interactions

Contact Info

Product

Resources

About