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Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin.

Garcia-Pino A, Buts L, Wyns L, Loris R
J Mol Biol 361 153-67 (2006)
Related entries: 2gme, 2gmm, 2gn3, 2gn7, 2gnb, 2gnd, 2gnm, 2gnt

Cited: 8 times
EuropePMC logo PMID: 16824540

Abstract

The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.

Reviews - 2gmp mentioned but not cited (1)

  1. Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi. Barre A, Bourne Y, Van Damme EJM, Rougé P. Int J Mol Sci 20 (2019)

Articles - 2gmp mentioned but not cited (1)

  1. How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity. Cuskin F, Flint JE, Gloster TM, Morland C, Baslé A, Henrissat B, Coutinho PM, Strazzulli A, Solovyova AS, Davies GJ, Gilbert HJ. Proc. Natl. Acad. Sci. U.S.A. 109 20889-20894 (2012)


Articles citing this publication (6)

  1. Molecular Basis for Recognition of the Cancer Glycobiomarker, LacdiNAc (GalNAc[β1→4]GlcNAc), by Wisteria floribunda Agglutinin. Haji-Ghassemi O, Gilbert M, Spence J, Schur MJ, Parker MJ, Jenkins ML, Burke JE, van Faassen H, Young NM, Evans SV. J. Biol. Chem. 291 24085-24095 (2016)
  2. How a plant lectin recognizes high mannose oligosaccharides. Garcia-Pino A, Buts L, Wyns L, Imberty A, Loris R. Plant Physiol. 144 1733-1741 (2007)
  3. The Rel stringent factor from Thermus thermophilus: crystallization and X-ray analysis. Van Nerom K, Tamman H, Takada H, Hauryliuk V, Garcia-Pino A. Acta Crystallogr F Struct Biol Commun 75 561-569 (2019)
  4. Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system. Jurėnas D, Van Melderen L, Garcia-Pino A. Nat. Chem. Biol. 15 285-294 (2019)
  5. Structure of SpoT reveals evolutionary tuning of catalysis via conformational constraint. Tamman H, Ernits K, Roghanian M, Ainelo A, Julius C, Perrier A, Talavera A, Ainelo H, Dugauquier R, Zedek S, Thureau A, Pérez J, Lima-Mendez G, Hallez R, Atkinson GC, Hauryliuk V, Garcia-Pino A. Nat Chem Biol 19 334-345 (2023)
  6. Staphylococcal Periscope proteins Aap, SasG, and Pls project noncanonical legume-like lectin adhesin domains from the bacterial surface. Clark LC, Atkin KE, Whelan F, Brentnall AS, Harris G, Towell AM, Turkenburg JP, Liu Y, Feizi T, Griffiths SC, Geoghegan JA, Potts JR. J Biol Chem 299 102936 (2023)


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