2q33: Difference between revisions

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[[Image:2q33.jpg|left|200px]]
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[[Image:2q33.png|left|200px]]


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{{STRUCTURE_2q33|  PDB=2q33  |  SCENE=  }}  
{{STRUCTURE_2q33|  PDB=2q33  |  SCENE=  }}  


'''Crystal structure of all-D monellin at 1.8 A resolution'''
===Crystal structure of all-D monellin at 1.8 A resolution===




==Overview==
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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.
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{{ABSTRACT_PUBMED_9867435}}


==About this Structure==
==About this Structure==
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[[Category: Alpha/beta]]
[[Category: Alpha/beta]]
[[Category: De novo protein]]
[[Category: De novo protein]]
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Revision as of 04:09, 29 July 2008

File:2q33.png

Template:STRUCTURE 2q33

Crystal structure of all-D monellin at 1.8 A resolution

Template:ABSTRACT PUBMED 9867435

About this Structure

2Q33 is a Protein complex structure. This structure supersedes 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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