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1bd7
From Proteopedia
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==CIRCULARLY PERMUTED BB2-CRYSTALLIN== | ==CIRCULARLY PERMUTED BB2-CRYSTALLIN== | ||
| - | <StructureSection load='1bd7' size='340' side='right' caption='[[1bd7]], [[Resolution|resolution]] 2.78Å' scene=''> | + | <StructureSection load='1bd7' size='340' side='right'caption='[[1bd7]], [[Resolution|resolution]] 2.78Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1bd7]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1bd7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BD7 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78Å</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=1bd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bd7 OCA], [https://pdbe.org/1bd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bd7 RCSB], [https://www.ebi.ac.uk/pdbsum/1bd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bd7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CRBB2_RAT CRBB2_RAT] Crystallins are the dominant structural components of the vertebrate eye lens. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/1bd7_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bd/1bd7_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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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=1bd7 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=1bd7 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly. | ||
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| - | Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly.,Wright G, Basak AK, Wieligmann K, Mayr EM, Slingsby C Protein Sci. 1998 Jun;7(6):1280-5. PMID:9655330<ref>PMID:9655330</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Crystallin 3D structures|Crystallin 3D structures]] | |
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| - | == | + | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Basak | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Glockshuber | + | [[Category: Basak AK]] |
| - | [[Category: Mayr | + | [[Category: Glockshuber R]] |
| - | [[Category: Slingsby | + | [[Category: Mayr E-M]] |
| - | [[Category: Wright | + | [[Category: Slingsby C]] |
| - | + | [[Category: Wright G]] | |
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Current revision
CIRCULARLY PERMUTED BB2-CRYSTALLIN
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