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Taxonomic group: plant / Streptophyta (Phylum: Streptophyta)
Organ / tissue: root

The structure was elucidated in this paper
NCBI PubMed ID: 9559667
Publication DOI: 10.1016/s0014-5793(98)00243-9
Journal NLM ID: 0155157
Publisher: Elsevier
Correspondence: Calvete JJ <jcalvete

repro.tiho-hannover.de>
Institutions: Institut für Reproduktionsmedizin, Tierärztliche Hochschule Hannover, Hannover-Kirchrode, Germany, Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil, Max-Planck-Institut für Biochemie, Martinsried, Germany, Gesellschaft für biotechnologische Forschung (GBF) mbH, Braunschweig, Germany, Biophysikalisch-biochemische Verfahren, Medizinische Hochschule, Hannover, Germany

VML is a galactose-binding lectin isolated from Vatairea macrocarpa seeds. By SDS-polyacrylamide gel electrophoresis, VML is a glycoprotein composed of a major 32-34 kDa double band (alpha-chain) and minor 22 kDa and 13 kDa bands. N-terminal sequencing of electroblotted samples showed that the 22 and 13 kDa bands corresponded to C-(beta) and N-(gamma) terminal fragments of the alpha-chain, respectively. The primary structure of VML displays similarity with other leguminous lectins, particularly with Erythrina variegata, Robinia pseudoacacia and Sophora japonica lectins. VML is N-glycosylated at asparagine residues at positions 111 and 183 with one major glycan structure. Tandem mass spectrometry and methylation analysis indicated the presence of Man alpha 1-6[(Man alpha 1-3)(Xyl beta 1-2)]Man beta 1-4-GlcNAc beta 1-4(Fuc alpha 1-3)GlcNAc, a typical plant N-glycan. Equilibrium sedimentation analysis by analytical centrifugation showed that VML had a mass of 122-130 kDa, which did not change within the pH range 2.5-8.5. These data indicated that VML is a pH-independent homotetrameric protein and that a small proportion of the alpha-subunits is cleaved into noncovalently associated N- and C-terminal fragments. Mass spectrometric analysis suggested a mechanism for the proteolytic processing of VML. V. macrocarpa lectin contains a mixture of doubly (28 525 Da) and singly (27 354 Da) glycosylated alpha-chains. Deglycosylation of Asn-111 correlates,vith proteolytic cleavage of the Asn-114-Lys-115 bond yielding glycosylated gamma (residues 1-114, 12 304 Da) and nonglycosylated beta-(residues 115-239, 14 957 Da) chains. Some beta-chain molecules are further deglycosylated and N-terminally processed yielding products of molecular masses of 13 783 Da and 13 670 Da.

mass spectrometry, carbohydrate structure, primary structure, Vatairea macrocarpa seed, galactose-binding leguminous lectin, posttranslational processing

Structure type: oligomer ; 1524
Location inside paper: Abstract
Aglycon: (->4) Asn-X-Ser/Thr (VML)
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145668,IEDB_145669,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_548907,IEDB_983930,SB_197,SB_198,SB_33,SB_44,SB_67,SB_72,SB_73,SB_74,SB_85,SB_86

Methods: ESI-MS, GC, methanolysis, extraction, permethylation, preacetylation
Comments, role: N-glycan moiety attached to Asn111 and Asn183

NCBI Taxonomy refs (TaxIDs): 77050
Reference(s) to other database(s): GTC:G80306BI
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There are 4 chemically distinct structures. Please, select:

CC(=O)N[C@H]1[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O)[C@H](NC(C)=O)[C@H]2O[C@H]2O[C@H](C)[C@H](O)[C@H](O)[C@H]2O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O)[C@@H](O)[C@H](O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O)[C@@H]2O[C@@H]2OC[C@@H](O)[C@H](O)[C@H]2O)[C@@H]1O

SVG MW SMILES 3D mol Ionize