2q33
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(New page: 200px<br /><applet load="2q33" size="450" color="white" frame="true" align="right" spinBox="true" caption="2q33, resolution 1.80Å" /> '''Crystal structure of...)
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Revision as of 06:41, 25 November 2007
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Crystal structure of all-D monellin at 1.8 A resolution
Overview
The D-enantiomer of a potently sweet protein, monellin, has been, crystallized and analyzed by X-ray crystallography at 1.8 A resolut ion., Two crystal forms (I and II) appeared under crystallization conditions, similar, but not identical, to the crystallization conditions of natural, L-monellin. There are four molecules per asymmetric unit in crystal form I, and one in crystal form II. Crystal form I is not reproducible and is, equivalent to that of monoclinic L-monellin. Intermonomer contacts in, crystal form II are very different from those found in natural L-monellin, crystals. The backbone trace of D-monellin resembles very closely the, mirror image of that of L-monellin, but the N- and C-terminus backbones as, well as several side-chain conformations of D-monellin are different from, those of natural L-monellin. Most of these apparent differences may be, attributable to the crystal packing differences.
About this Structure
2Q33 is a Protein complex structure of sequences from [1]. This structure superseeds the now removed PDB entry 1N98. Full crystallographic information is available from OCA.
Reference
Structure of an enantiomeric protein, D-monellin at 1.8 A resolution., Hung LW, Kohmura M, Ariyoshi Y, Kim SH, Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):494-500. PMID:9867435
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