2gnm

P. angolensis lectin (PAL) treated with EDTA for 39 hours

spinqualitylabelsall models 2gnm, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2gnm is a 2 chain structure with sequence from Pterocarpus angolensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: CA, MAN, MN, PCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8GSD2_PTEAG Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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. 2006 Aug 4;361(1):153-67. Epub 2006 Jun 21. PMID:16824540 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pal

Proteopedia Page Contributors and Editors (what is this?)

OCA