4mon
From Proteopedia
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ORTHORHOMBIC MONELLIN
Overview
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.
About this Structure
4MON is a Protein complex structure of sequences from Dioscoreophyllum cumminsii. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Tue Nov 20 19:43:12 2007
