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2q33
From Proteopedia
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| - | [[Image:2q33.jpg|left|200px]] | ||
| - | + | ==Crystal structure of all-D monellin at 1.8 A resolution== | |
| - | + | <StructureSection load='2q33' size='340' side='right'caption='[[2q33]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2q33]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1n98 1n98]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q33 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=DAS:D-ASPARTIC+ACID'>DAS</scene>, <scene name='pdbligand=DCY:D-CYSTEINE'>DCY</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=DGN:D-GLUTAMINE'>DGN</scene>, <scene name='pdbligand=DIL:D-ISOLEUCINE'>DIL</scene>, <scene name='pdbligand=DLE:D-LEUCINE'>DLE</scene>, <scene name='pdbligand=DLY:D-LYSINE'>DLY</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=DSG:D-ASPARAGINE'>DSG</scene>, <scene name='pdbligand=DSN:D-SERINE'>DSN</scene>, <scene name='pdbligand=DTH:D-THREONINE'>DTH</scene>, <scene name='pdbligand=DTR:D-TRYPTOPHAN'>DTR</scene>, <scene name='pdbligand=DTY:D-TYROSINE'>DTY</scene>, <scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=MED:D-METHIONINE'>MED</scene></td></tr> | |
| - | --> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2q33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q33 OCA], [https://pdbe.org/2q33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q33 RCSB], [https://www.ebi.ac.uk/pdbsum/2q33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q33 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | ''' | + | == Publication Abstract from PubMed == |
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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. | 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. | ||
| - | + | 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<ref>PMID:9867435</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2q33" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ariyoshi | + | == References == |
| - | [[Category: Hung | + | <references/> |
| - | [[Category: Kim | + | __TOC__ |
| - | [[Category: Kohmura | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Ariyoshi Y]] | |
| - | + | [[Category: Hung L-W]] | |
| - | + | [[Category: Kim S-H]] | |
| + | [[Category: Kohmura M]] | ||
Current revision
Crystal structure of all-D monellin at 1.8 A resolution
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