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2GMM

Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-2)Man

Summary for 2GMM
Entry DOI10.2210/pdb2gmm/pdb
Related1UKG 2GME
Related PRD IDPRD_900111
Descriptorlectin, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, SULFATE ION, ... (4 entities in total)
Functional Keywordslegume lectin, metal-free lectin, sugar complex, man2man, beta sandwich, sugar binding protein
Biological sourcePterocarpus angolensis
Total number of polymer chains2
Total formula weight55993.31
Authors
Garcia-Pino, A.,Buts, L.,Wyns, L.,Loris, R. (deposition date: 2006-04-07, release date: 2006-07-25, Last modification date: 2024-10-30)
Primary citationGarcia-Pino, A.,Buts, L.,Wyns, L.,Loris, R.
Interplay Between Metal Binding and cis/trans Isomerization in Legume Lectins: Structural and Thermodynamic Study of P. angolensis Lectin.
J.Mol.Biol., 361:153-167, 2006
Cited by
PubMed 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.
PubMed: 16824540
DOI: 10.1016/j.jmb.2006.06.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

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