4mon | pdb_00004mon

ORTHORHOMBIC MONELLIN

spinqualitylabelsall models 4mon, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4mon is a 4 chain structure with sequence from Dioscoreophyllum cumminsii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed The structure of orthorhombic crystals of monellin, a sweet protein extracted from African serendipity berries, has been solved by molecular replacement and refined to 2.3 A resolution. The final R factor was 0.150 for a model with excellent geometry. A monellin molecule consists of two peptides that are non-covalently bound, with chain A composed of three beta-strands interconnected by loop regions and chain B composed of two beta-strands interconnected by an alpha-helix. The N terminus of chain A is in close proximity to the C terminus of chain B. The two molecules in the asymmetric unit are related by a non-crystallographic twofold axis and form a dimer, similar to those previously observed in other crystal forms of both natural and single-chain monellin. The r.m.s, deviation between the Calpha atoms in the two independent molecules is 0.60 A, while the deviations from the individual molecules in the previously reported monoclinic crystals are 0.50-0.57 A. This result proves that the structure of monellin is not significantly influenced by crystal packing forces. Structure of monellin refined to 2.3 a resolution in the orthorhombic crystal form.,Bujacz G, Miller M, Harrison R, Thanki N, Gilliland GL, Ogata CM, Kim SH, Wlodawer A Acta Crystallogr D Biol Crystallogr. 1997 Nov 1;53(Pt 6):713-9. PMID:15299859 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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