Carboxylesterase
From Proteopedia
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Regions of the current structure that differ from the previously reported examples of hCES1 include Ser365–Asp374, which has very poor density. In the [[2h7c]] structure <scene name='Journal:Acta_Cryst_F:1/Cv/12'>each of the six examples of the section of chain from Ser365 to Asp374 has a different conformation</scene>. The poorly defined density for this same region in rhCES1 is consistent with the observation that <scene name='Journal:Acta_Cryst_F:1/Cv/13'>this loop can adopt multiple conformations despite its participation in forming the twofold interface between chains</scene> (<font color='red'><b>the loop of one subunit is in red</b></font> and <span style="color:orange;background-color:black;font-weight:bold;">the loop of the second subunit is in orange</span>). | Regions of the current structure that differ from the previously reported examples of hCES1 include Ser365–Asp374, which has very poor density. In the [[2h7c]] structure <scene name='Journal:Acta_Cryst_F:1/Cv/12'>each of the six examples of the section of chain from Ser365 to Asp374 has a different conformation</scene>. The poorly defined density for this same region in rhCES1 is consistent with the observation that <scene name='Journal:Acta_Cryst_F:1/Cv/13'>this loop can adopt multiple conformations despite its participation in forming the twofold interface between chains</scene> (<font color='red'><b>the loop of one subunit is in red</b></font> and <span style="color:orange;background-color:black;font-weight:bold;">the loop of the second subunit is in orange</span>). | ||
The current results confirm that rhHCES1 isolated from the ''T. ni'' system is essentially identical to previous examples of this enzyme isolated from cultured insect cells, validating the use of the whole insect system as a source for recombinant proteins in structure determination studies.<ref >doi:10.1107/S1744309112003326</ref><br /> | The current results confirm that rhHCES1 isolated from the ''T. ni'' system is essentially identical to previous examples of this enzyme isolated from cultured insect cells, validating the use of the whole insect system as a source for recombinant proteins in structure determination studies.<ref >doi:10.1107/S1744309112003326</ref><br /> | ||
| - | '''Palmitoleoyl-protein carboxyl esterase NOTUM''' mediates depalmitolyation of | + | '''Palmitoleoyl-protein carboxyl esterase NOTUM''' mediates depalmitolyation of Wnt proteins<ref>PMID:25731175</ref>. |
Current revision
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References
- ↑ Greenblatt HM, Otto TC, Kirkpatrick MG, Kovaleva E, Brown S, Buchman G, Cerasoli DM, Sussman JL. Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):269-72., Epub 2012 Feb 15. PMID:22442219 doi:10.1107/S1744309112003326
- ↑ Kakugawa S, Langton PF, Zebisch M, Howell SA, Chang TH, Liu Y, Feizi T, Bineva G, O'Reilly N, Snijders AP, Jones EY, Vincent JP. Notum deacylates Wnt proteins to suppress signalling activity. Nature. 2015 Mar 12;519(7542):187-92. doi: 10.1038/nature14259. Epub 2015 Feb 25. PMID:25731175 doi:http://dx.doi.org/10.1038/nature14259
