6v7g | pdb_00006v7g

Binding of Benzoic Acid and Anions Within the Cupin Domains of the Vicillin Protein Canavalin from Jack Bean (canavalia ensiformis): Crystal Structures

spinqualitylabelsall models 6v7g, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6v7g is a 1 chain structure with sequence from Canavalia ensiformis. This structure supersedes the now removed PDB entry 6cb4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.4Å Ligands: ACT, BEZ, CIT, OCS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CANA_CANEN Seed storage protein. Publication Abstract from PubMed X-ray intensities extending to 1.4 A resolution were collected on the P63 hexagonal crystal form of canavalin, and extended to 1.9 A for the orthorhombic C2221 crystals. Structure determination of a new crystal form of canavalin having space group P212121 is reported as well. Both the N and C terminal cupin domains contained identifiable ligands. For hexagonal crystals, in the cavity of the C terminal cupin, a molecule of benzoic acid was found, bound through carboxyl oxygens to Histidine 297, asparagine 284 and Arginine 376. The benzene ring was immersed in a cluster of at least 8 hydrophobic amino acid side chains. The N terminal cupin contained a molecule of citrate. Benzoic acid was also found to be present in the C terminal cupins of in the C2221 and P212121 crystal forms. In rhombohedral crystals, the C terminal cupin domain appeared to be occupied by a phosphate ion, but this was ambiguous. In cubic crystals, both domains were vacant. The N terminal cupin domains of canavalin in the P212121 and rhombohedral crystals were also vacant, but the N terminal cupin domain of the C2221 crystals contained a ligand whose identity is uncertain, but which has been modeled as HEPES buffer. A possible physiological role for the ligands and their complexes with canavalin is considered. Binding of benzoic acid and anions within the cupin domains of the vicilin protein canavalin from jack bean (Canavalia ensiformis): Crystal structures.,McPherson A Biochem Biophys Res Commun. 2020 Jan 23. pii: S0006-291X(20)30176-5. doi:, 10.1016/j.bbrc.2020.01.101. PMID:31983433 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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