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1DQ1

Calcium;Calcium concanavalin A

Summary for 1DQ1
Entry DOI10.2210/pdb1dq1/pdb
Related1DQ0 1DQ2 1DQ4 1DQ5 1DQ6
DescriptorConcanavalin-Br, CALCIUM ION (3 entities in total)
Functional Keywordsbeta-sheet, leguminosae lectin, calcium, transition metal, ion binding site, s1, calcium binding site, s2, sugar binding protein
Biological sourceCanavalia ensiformis (jack bean)
Total number of polymer chains1
Total formula weight25702.54
Authors
Bouckaert, J.,Dewallef, Y.,Poortmans, F.,Wyns, L.,Loris, R. (deposition date: 1999-12-29, release date: 2000-01-19, Last modification date: 2024-02-07)
Primary citationBouckaert, J.,Dewallef, Y.,Poortmans, F.,Wyns, L.,Loris, R.
The structural features of concanavalin A governing non-proline peptide isomerization
J.Biol.Chem., 275:19778-19787, 2000
Cited by
PubMed Abstract: The reversible binding of manganese and calcium to concanavalin A determines the carbohydrate binding of the lectin by inducing large conformational changes. These changes are governed by the isomerization of a non-proline peptide bond, Ala-207-Asp-208, positioned in a beta-strand in between the calcium binding site S2 and the carbohydrate specificity-determining loop. The replacement of calcium by manganese allowed us to investigate the structures of the carbohydrate binding, locked state and the inactive, unlocked state of concanavalin A, both with and without metal ions bound. Crystals of unlocked metal-free concanavalin A convert to the locked form with the binding of two Mn(2+) ions. Removal of these ions from the crystals traps metal-free concanavalin A in its locked state, a minority species in solution. The ligation of a metal ion in S2 to unlocked concanavalin A causes bending of the beta-strand foregoing the S2 ligand residues Asp-10 and Tyr-12. This bending disrupts conventional beta-sheet hydrogen bonding and forces the Thr-11 side chain against the Ala-207-Asp-208 peptide bond. The steric strain exerted by Thr-11 is presumed to drive the trans-to-cis isomerization. Upon isomerization, Asp-208 flips into its carbohydrate binding position, and the conformation of the carbohydrate specificity determining loop changes dramatically.
PubMed: 10748006
DOI: 10.1074/jbc.M001251200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.15 Å)
Structure validation

226707

數據於2024-10-30公開中

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