{"refrec":{"BRefID":261275,"RR":"<b>Tan, W.-H.; Cheng, S.-C.; Liu, Y.-T.; Wu, C.-G.; Lin, M.-H.; Chen, C.-C.; Lin, C.-H.; Chou, C.-Y.</b> (2016). Structure of a highly active cephalopod S-crystallin mutant: New molecular evidence for evolution from an active enzyme into lens-refractive protein. <i>NPG Scientific Reports 6(31176)</i>: 9 pp. <a href=\"http://dx.doi.org/10.1038/srep31176\" target=\"_blank\">http://dx.doi.org/10.1038/srep31176</a>","BEntID":253293,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>NPG Scientific Reports 6(31176)</i>: 9 pp. <a href=\"http://dx.doi.org/10.1038/srep31176\" target=\"_blank\">http://dx.doi.org/10.1038/srep31176</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Tan, W.-H.; Cheng, S.-C.; Liu, Y.-T.; Wu, C.-G.; Lin, M.-H.; Chen, C.-C.; Lin, C.-H.; Chou, C.-Y.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Tan, W.-H. <i>et al.</i>","Englishabstract":"Crystallins are found widely in animal lenses and have important functions due to their refractive properties. In the coleoid cephalopods, a lens with a graded refractive index provides good vision and is required for survival. Cephalopod S-crystallin is thought to have evolved from glutathione S-transferase (GST) with various homologs differentially expressed in the lens. However, there is no direct structural information that helps to delineate the mechanisms by which S-crystallin could have evolved. Here we report the structural and biochemical characterization of novel S-crystallin-glutathione complex. The 2.35-A crystal structure of a-crystallin mutant from Octopus vulgaris reveals an active-site architecture that is different from that of GST. S-crystallin has a preference for glutathione binding, although almost lost its GST enzymatic activity. We've also identified four historical mutations that are able to produce a \"GST-like\" S-crystallin that has regained activity. This protein recapitulates the evolution of S-crystallin from GST. Protein stability studies suggest that S-crystallin is stabilized by glutathione binding to prevent its aggregation; this contrasts with GST-sigma, which do not possess this protection. We suggest that a tradeoff between enzyme activity and the stability of the lens protein might have been one of the major driving force behind lens evolution.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Structure of a highly active cephalopod S-crystallin mutant: New molecular evidence for evolution from an active enzyme into lens-refractive protein","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-10 01:32:01.350754","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2016,"MonPub":null,"DateUpdate":"2018-02-13","DateCreate":"2016-09-07","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000392101500001","VABBcode":null,"OpenAcc":1,"DOI":"10.1038/srep31176"},"refs":null,"anarec":{"AnaID":261275,"PubliDate":2016,"Pagination":"9 pp","XtraPublOfAnaID":null,"ISBN":null,"Volume":"6","Issue":"31176","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":208093,"SerRR":"Scientific Reports (Nature Publishing Group). 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