Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Rosana Simón-Vázquez, Marta Domínguez, Víctor A Lórenz-Fonfría, Susana Alvarez, José-Luís Bourdelande, Angel R de Lera, Esteve Padrós, Alex Perálvarez-Marín
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8dbfd59be4ea49ff9d2753dd0fd882cf
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:8dbfd59be4ea49ff9d2753dd0fd882cf
record_format	dspace
spelling	oai:doaj.org-article:8dbfd59be4ea49ff9d2753dd0fd882cf2021-11-18T07:09:45ZProbing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.1932-620310.1371/journal.pone.0042447https://doaj.org/article/8dbfd59be4ea49ff9d2753dd0fd882cf2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22879987/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoproteins with all-trans-retinal and its 20-methyl derivative (hereafter, 13-ethyl retinal). Biophysical characterization indicates that recovering the steric interaction between the residue 90 and retinal, eases the accommodation of the chromophore, however it is not enough for a complete phenotype rescue. The characterization of these chemically engineered chromoproteins provides further insight into the role of the hydrogen bond network and the steric interactions involving the retinal binding pocket in bacteriorhodopsin and other microbial sensory rhodopsins.Rosana Simón-VázquezMarta DomínguezVíctor A Lórenz-FonfríaSusana AlvarezJosé-Luís BourdelandeAngel R de LeraEsteve PadrósAlex Perálvarez-MarínPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 8, p e42447 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rosana Simón-Vázquez Marta Domínguez Víctor A Lórenz-Fonfría Susana Alvarez José-Luís Bourdelande Angel R de Lera Esteve Padrós Alex Perálvarez-Marín Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
description	Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoproteins with all-trans-retinal and its 20-methyl derivative (hereafter, 13-ethyl retinal). Biophysical characterization indicates that recovering the steric interaction between the residue 90 and retinal, eases the accommodation of the chromophore, however it is not enough for a complete phenotype rescue. The characterization of these chemically engineered chromoproteins provides further insight into the role of the hydrogen bond network and the steric interactions involving the retinal binding pocket in bacteriorhodopsin and other microbial sensory rhodopsins.
format	article
author	Rosana Simón-Vázquez Marta Domínguez Víctor A Lórenz-Fonfría Susana Alvarez José-Luís Bourdelande Angel R de Lera Esteve Padrós Alex Perálvarez-Marín
author_facet	Rosana Simón-Vázquez Marta Domínguez Víctor A Lórenz-Fonfría Susana Alvarez José-Luís Bourdelande Angel R de Lera Esteve Padrós Alex Perálvarez-Marín
author_sort	Rosana Simón-Vázquez
title	Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
title_short	Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
title_full	Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
title_fullStr	Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
title_full_unstemmed	Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
title_sort	probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/8dbfd59be4ea49ff9d2753dd0fd882cf
work_keys_str_mv	AT rosanasimonvazquez probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT martadominguez probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT victoralorenzfonfria probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT susanaalvarez probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT joseluisbourdelande probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT angelrdelera probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT estevepadros probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach AT alexperalvarezmarin probingapolarclusterintheretinalbindingpocketofbacteriorhodopsinbyachemicaldesignapproach
_version_	1718423864394907648

Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach.

Ejemplares similares