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| ==Red abalone lysin F104A== | | ==Red abalone lysin F104A== |
| <StructureSection load='5utg' size='340' side='right' caption='[[5utg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='5utg' size='340' side='right'caption='[[5utg]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5utg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/California_red_abalone California red abalone]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UTG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UTG FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5utg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliotis_rufescens Haliotis rufescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UTG FirstGlance]. <br> |
| </td></tr><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=5utg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5utg OCA], [http://pdbe.org/5utg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5utg RCSB], [http://www.ebi.ac.uk/pdbsum/5utg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5utg ProSAT]</span></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5utg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5utg OCA], [https://pdbe.org/5utg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5utg RCSB], [https://www.ebi.ac.uk/pdbsum/5utg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5utg ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ELYS_HALRU ELYS_HALRU]] Dissolves the egg vitelline layer nonenzymatically during fertilization. It creates a hole of about 3 mu-m in diameter through which the sperm pass. | | [https://www.uniprot.org/uniprot/ELYS_HALRU ELYS_HALRU] Dissolves the egg vitelline layer nonenzymatically during fertilization. It creates a hole of about 3 mu-m in diameter through which the sperm pass. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Protein evolution is driven by the sum of different physiochemical and genetic processes that usually results in strong purifying selection to maintain biochemical functions. However, proteins that are part of systems under arms race dynamics often evolve at unparalleled rates that can produce atypical biochemical properties. In the marine mollusk abalone, lysin and vitelline envelope receptor for lysin (VERL) are a pair of rapidly coevolving proteins that are essential for species-specific interactions between sperm and egg. Despite extensive biochemical characterization of lysin-including crystal structures of multiple orthologs-it was unclear how sites under positive selection may facilitate recognition of VERL. Using a combination of targeted mutagenesis and multidimensional NMR, we present a high-definition solution structure of sperm lysin from red abalone (Haliotis rufescens). Unapparent from the crystallography data, multiple NMR-based analyses conducted in solution reveal clustering of the N and C termini to form a nexus of 13 positively selected sites that constitute a VERL binding interface. Evolutionary rate was found to be a significant predictor of backbone flexibility, which may be critical for lysin bioactivity and/or accelerated evolution. Flexible, rapidly evolving segments that constitute the VERL binding interface were also the most distorted regions of the crystal structure relative to what was observed in solution. While lysin has been the subject of extensive biochemical and evolutionary analyses for more than 30 years, this study highlights the enhanced insights gained from applying NMR approaches to rapidly evolving proteins.
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| Solution structure of sperm lysin yields novel insights into molecular dynamics of rapid protein evolution.,Wilburn DB, Tuttle LM, Klevit RE, Swanson WJ Proc Natl Acad Sci U S A. 2018 Jan 18. pii: 1709061115. doi:, 10.1073/pnas.1709061115. PMID:29348201<ref>PMID:29348201</ref>
| | ==See Also== |
| | | *[[Lysin 3D structures|Lysin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5utg" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: California red abalone]] | | [[Category: Haliotis rufescens]] |
| [[Category: Tuttle, L M]] | | [[Category: Large Structures]] |
| [[Category: Wilburn, D B]] | | [[Category: Tuttle LM]] |
| [[Category: Cell adhesion]] | | [[Category: Wilburn DB]] |
| [[Category: Fertilization protein]]
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