4mon
From Proteopedia
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| - | [[Image:4mon.gif|left|200px]] | + | [[Image:4mon.gif|left|200px]] |
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| - | '''ORTHORHOMBIC MONELLIN''' | + | {{Structure |
| + | |PDB= 4mon |SIZE=350|CAPTION= <scene name='initialview01'>4mon</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ORTHORHOMBIC MONELLIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 4MON is a [ | + | 4MON is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MON OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299859 15299859] |
[[Category: Dioscoreophyllum cumminsii]] | [[Category: Dioscoreophyllum cumminsii]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bujacz, G.]] | [[Category: Bujacz, G.]] | ||
[[Category: Wlodawer, A.]] | [[Category: Wlodawer, A.]] | ||
| - | [[Category: orthorhombic | + | [[Category: orthorhombic crystal]] |
[[Category: sweet-tasting protein]] | [[Category: sweet-tasting protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:19 2008'' |
Revision as of 17:10, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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