1pp3

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<StructureSection load='1pp3' size='340' side='right'caption='[[1pp3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1pp3' size='340' side='right'caption='[[1pp3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1pp3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Katemfe Katemfe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PP3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1pp3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thaumatococcus_daniellii Thaumatococcus daniellii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PP3 FirstGlance]. <br>
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</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=1pp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pp3 OCA], [https://pdbe.org/1pp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pp3 RCSB], [https://www.ebi.ac.uk/pdbsum/1pp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pp3 ProSAT]</span></td></tr>
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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]] 1.6&#8491;</td></tr>
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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=1pp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pp3 OCA], [https://pdbe.org/1pp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pp3 RCSB], [https://www.ebi.ac.uk/pdbsum/1pp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pp3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA]] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
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[https://www.uniprot.org/uniprot/THM1_THADA THM1_THADA] Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pp3 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1pp3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The intensely sweet protein thaumatin has been crystallized in a hexagonal lattice after a temperature shift from 293 to 277 K. The structure of the protein in the new crystal was solved at 1.6 A resolution. The protein fold is identical to that found in three other crystal forms grown in the presence of crystallizing agents of differing chemical natures. The proportions of lattice interactions involving hydrogen bonds, hydrophobic or ionic groups differ greatly from one form to another. Moreover, the distribution of acidic and basic residues taking part in contacts also varies. The hexagonal packing is characterized by the presence of channels parallel to the c axis that are so wide that protein molecules can diffuse through them.
 
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Structure of thaumatin in a hexagonal space group: comparison of packing contacts in four crystal lattices.,Charron C, Giege R, Lorber B Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):83-9. Epub 2003 Dec, 18. PMID:14684896<ref>PMID:14684896</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1pp3" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Katemfe]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Charron, C]]
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[[Category: Thaumatococcus daniellii]]
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[[Category: Giege, R]]
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[[Category: Charron C]]
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[[Category: Lorber, B]]
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[[Category: Giege R]]
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[[Category: Plant protein]]
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[[Category: Lorber B]]

Revision as of 05:57, 17 April 2024

Structure of thaumatin in a hexagonal space group

PDB ID 1pp3

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