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4fd9

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==Crystal structure of the third beta-gamma-crystallin domain of Crybg3 (betagamma-crystallin domain-containing protein 3) from Mus musculus==
==Crystal structure of the third beta-gamma-crystallin domain of Crybg3 (betagamma-crystallin domain-containing protein 3) from Mus musculus==
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<StructureSection load='4fd9' size='340' side='right' caption='[[4fd9]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='4fd9' size='340' side='right'caption='[[4fd9]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4fd9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FD9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4fd9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FD9 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cw3|3cw3]]</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]] 1.86&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Crybg3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=4fd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fd9 OCA], [https://pdbe.org/4fd9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fd9 RCSB], [https://www.ebi.ac.uk/pdbsum/4fd9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fd9 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fd9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fd9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fd9 RCSB], [http://www.ebi.ac.uk/pdbsum/4fd9 PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/CRBG3_MOUSE CRBG3_MOUSE]
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The folding and unfolding of structurally similar proteins belonging to a family have long been a focus of investigation of the structure-(un)folding relationship. Such studies are yet to reach a consensus about whether structurally similar domains follow common or different unfolding pathways. Members of the betagamma-crystallin superfamily, which consists of structurally similar proteins with limited sequence similarity from diverse life forms spanning microbes to mammals, form an appropriate model system for exploring this relationship further. We selected a new member, Crybg3_D3, the third betagamma-crystallin domain of non-lens vertebrate protein Crybg3 from mouse brain. The crystal structure determined at 1.86 A demonstrates that the betagamma-crystallin domain of Crybg3 resembles more closely the lens betagamma-crystallins than the microbial crystallins do. However, interestingly, this structural cousin follows a quite distinct (un)folding pathway via formation of an intermediate state. The intermediate species is in a nativelike conformation with variation in flexibility and tends to form insoluble aggregates. The individual domains of lens betagamma-crystallins (and microbial homologues) do not follow such an unfolding pattern. Thus, even the closest members of a subfamily within a superfamily do not necessarily follow similar unfolding paths, suggesting the divergence acquired by these domains, which could be observed only by unfolding. Additionally, this study provides insights into the modifications that this domain has undergone during its recruitment into the non-lens tissues in vertebrates.
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Aggregation-prone near-native intermediate formation during unfolding of a structurally similar nonlenticular betagamma-crystallin domain.,Rajanikanth V, Srivastava SS, Singh AK, Rajyalakshmi M, Chandra K, Aravind P, Sankaranarayanan R, Sharma Y Biochemistry. 2012 Oct 30;51(43):8502-13. doi: 10.1021/bi300844u. Epub 2012 Oct, 18. PMID:23043265<ref>PMID:23043265</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Aravind, P]]
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[[Category: Aravind P]]
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[[Category: Sankaranarayanan, R]]
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[[Category: Sankaranarayanan R]]
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[[Category: Srivastava, S S]]
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[[Category: Srivastava SS]]
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[[Category: Brain]]
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[[Category: Non-lens vertebrate beta-gamma-crystallin]]
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[[Category: Structural protein]]
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Current revision

Crystal structure of the third beta-gamma-crystallin domain of Crybg3 (betagamma-crystallin domain-containing protein 3) from Mus musculus

PDB ID 4fd9

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