5utg

<StructureSection load='5utg' size='340' side='right' caption='[[5utg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[5utg]] is a 1 chain structure. 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>

</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>

[[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.

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.

 

== References ==

[[Category: Tuttle, L M]]

[[Category: Wilburn, D B]]

[[Category: Cell adhesion]]

[[Category: Fertilization protein]]