7rj0: Difference between revisions
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==Mouse Gamma S Crystallin L16 Octamer== | ==Mouse Gamma S Crystallin L16 Octamer== | ||
<StructureSection load='7rj0' size='340' side='right'caption='[[7rj0]]' scene=''> | <StructureSection load='7rj0' size='340' side='right'caption='[[7rj0]], [[Resolution|resolution]] 2.92Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6myh 6myh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RJ0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7rj0]] is a 4 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6myh 6myh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RJ0 FirstGlance]. <br> | ||
</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=7rj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rj0 OCA], [https://pdbe.org/7rj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rj0 RCSB], [https://www.ebi.ac.uk/pdbsum/7rj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rj0 ProSAT]</span></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7rj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rj0 OCA], [https://pdbe.org/7rj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rj0 RCSB], [https://www.ebi.ac.uk/pdbsum/7rj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rj0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/CRYGS_MOUSE CRYGS_MOUSE]] Crystallins are the dominant structural components of the vertebrate eye lens. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Misfolding and aggregation of proteins occur in many pathological states. Because of the inherent disorder involved, these processes are difficult to study. We attempted to capture aggregation intermediates of gammaS-crystallin, a highly stable, internally symmetrical monomeric protein, by crystallization under mildly acidic and oxidizing conditions. Here we describe novel oligomerization through strained domain-swapping and partial intermolecular disulfide formation. This forms an octamer built from asymmetric tetramers, each of which comprises an asymmetric pair of twisted, domain-swapped dimers. Each tetramer shows patterns of acquired disorder among subunits, ranging from local loss of secondary structure to regions of intrinsic disorder. The octamer ring is tied together by partial intermolecular disulfide bonds, which may contribute to strain and disorder in the octamer. Oligomerization in this structure is self-limited by the distorted octamer ring. In a more heterogeneous environment, the disordered regions could serve as seeds for cascading interactions with other proteins. Indeed, solubilized protein from crystals retain many features observed in the crystal and are prone to further oligomerization and precipitation. This structure illustrates modes of loss of organized structure and aggregation that are relevant for cataract and for other disorders involving deposition of formerly well-folded proteins. | |||
Acquired Disorder and Asymmetry in a Domain-Swapped Model for gamma-Crystallin Aggregation.,Sagar V, Wistow G J Mol Biol. 2022 Mar 24;434(9):167559. doi: 10.1016/j.jmb.2022.167559. PMID:35341744<ref>PMID:35341744</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7rj0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Sagar V]] | [[Category: Sagar, V]] | ||
[[Category: Disorder]] | |||
[[Category: Domain-swap]] | |||
[[Category: Octamer]] | |||
[[Category: Oxidation]] | |||
[[Category: Protein binding]] | |||
[[Category: Structural protein]] | |||
Revision as of 06:08, 21 April 2022
Mouse Gamma S Crystallin L16 OctamerMouse Gamma S Crystallin L16 Octamer
Structural highlights
Function[CRYGS_MOUSE] Crystallins are the dominant structural components of the vertebrate eye lens. Publication Abstract from PubMedMisfolding and aggregation of proteins occur in many pathological states. Because of the inherent disorder involved, these processes are difficult to study. We attempted to capture aggregation intermediates of gammaS-crystallin, a highly stable, internally symmetrical monomeric protein, by crystallization under mildly acidic and oxidizing conditions. Here we describe novel oligomerization through strained domain-swapping and partial intermolecular disulfide formation. This forms an octamer built from asymmetric tetramers, each of which comprises an asymmetric pair of twisted, domain-swapped dimers. Each tetramer shows patterns of acquired disorder among subunits, ranging from local loss of secondary structure to regions of intrinsic disorder. The octamer ring is tied together by partial intermolecular disulfide bonds, which may contribute to strain and disorder in the octamer. Oligomerization in this structure is self-limited by the distorted octamer ring. In a more heterogeneous environment, the disordered regions could serve as seeds for cascading interactions with other proteins. Indeed, solubilized protein from crystals retain many features observed in the crystal and are prone to further oligomerization and precipitation. This structure illustrates modes of loss of organized structure and aggregation that are relevant for cataract and for other disorders involving deposition of formerly well-folded proteins. Acquired Disorder and Asymmetry in a Domain-Swapped Model for gamma-Crystallin Aggregation.,Sagar V, Wistow G J Mol Biol. 2022 Mar 24;434(9):167559. doi: 10.1016/j.jmb.2022.167559. PMID:35341744[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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