4mon

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[[Image:4mon.gif|left|200px]]
 
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{{Structure
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==ORTHORHOMBIC MONELLIN==
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|PDB= 4mon |SIZE=350|CAPTION= <scene name='initialview01'>4mon</scene>, resolution 2.3&Aring;
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<StructureSection load='4mon' size='340' side='right'caption='[[4mon]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[4mon]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MON FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mon OCA], [https://pdbe.org/4mon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mon RCSB], [https://www.ebi.ac.uk/pdbsum/4mon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mon ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mon OCA], [http://www.ebi.ac.uk/pdbsum/4mon PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4mon RCSB]</span>
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[https://www.uniprot.org/uniprot/MONA_DIOCU MONA_DIOCU] Taste-modifying protein; intensely sweet-tasting protein.
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}}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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'''ORTHORHOMBIC MONELLIN'''
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==Overview==
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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.
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.
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==About this Structure==
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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<ref>PMID:15299859</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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<div class="pdbe-citations 4mon" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Dioscoreophyllum cumminsii]]
[[Category: Dioscoreophyllum cumminsii]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bujacz, G.]]
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[[Category: Bujacz G]]
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[[Category: Wlodawer, A.]]
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[[Category: Wlodawer A]]
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[[Category: orthorhombic crystal]]
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[[Category: sweet-tasting protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:39:28 2008''
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ORTHORHOMBIC MONELLIN

PDB ID 4mon

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