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Structural insights and ab initio sequencing within the DING proteins family

DING proteins constitute an intriguing family of phosphate-binding proteins that was identified in a wide range of organisms, from prokaryotes and archae to eukaryotes. Despite their seemingly ubiquitous occurrence in eukaryotes, their encoding genes are missing from sequenced genomes. Such a lack h...

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Detalles Bibliográficos
Autores principales: Elias, Mikael, Liebschner, Dorothee, Gotthard, Guillaume, Chabriere, Eric
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004253/
https://www.ncbi.nlm.nih.gov/pubmed/21169690
http://dx.doi.org/10.1107/S0909049510036009
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author Elias, Mikael
Liebschner, Dorothee
Gotthard, Guillaume
Chabriere, Eric
author_facet Elias, Mikael
Liebschner, Dorothee
Gotthard, Guillaume
Chabriere, Eric
author_sort Elias, Mikael
collection PubMed
description DING proteins constitute an intriguing family of phosphate-binding proteins that was identified in a wide range of organisms, from prokaryotes and archae to eukaryotes. Despite their seemingly ubiquitous occurrence in eukaryotes, their encoding genes are missing from sequenced genomes. Such a lack has considerably hampered functional studies. In humans, these proteins have been related to several diseases, like atherosclerosis, kidney stones, inflammation processes and HIV inhibition. The human phosphate binding protein is a human representative of the DING family that was serendipitously discovered from human plasma. An original approach was developed to determine ab initio the complete and exact sequence of this 38 kDa protein by utilizing mass spectrometry and X-ray data in tandem. Taking advantage of this first complete eukaryotic DING sequence, a immunohistochemistry study was undertaken to check the presence of DING proteins in various mice tissues, revealing that these proteins are widely expressed. Finally, the structure of a bacterial representative from Pseudomonas fluorescens was solved at sub-angstrom resolution, allowing the molecular mechanism of the phosphate binding in these high-affinity proteins to be elucidated.
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spelling pubmed-30042532010-12-23 Structural insights and ab initio sequencing within the DING proteins family Elias, Mikael Liebschner, Dorothee Gotthard, Guillaume Chabriere, Eric J Synchrotron Radiat Diffraction Structural Biology DING proteins constitute an intriguing family of phosphate-binding proteins that was identified in a wide range of organisms, from prokaryotes and archae to eukaryotes. Despite their seemingly ubiquitous occurrence in eukaryotes, their encoding genes are missing from sequenced genomes. Such a lack has considerably hampered functional studies. In humans, these proteins have been related to several diseases, like atherosclerosis, kidney stones, inflammation processes and HIV inhibition. The human phosphate binding protein is a human representative of the DING family that was serendipitously discovered from human plasma. An original approach was developed to determine ab initio the complete and exact sequence of this 38 kDa protein by utilizing mass spectrometry and X-ray data in tandem. Taking advantage of this first complete eukaryotic DING sequence, a immunohistochemistry study was undertaken to check the presence of DING proteins in various mice tissues, revealing that these proteins are widely expressed. Finally, the structure of a bacterial representative from Pseudomonas fluorescens was solved at sub-angstrom resolution, allowing the molecular mechanism of the phosphate binding in these high-affinity proteins to be elucidated. International Union of Crystallography 2011-01-01 2010-11-05 /pmc/articles/PMC3004253/ /pubmed/21169690 http://dx.doi.org/10.1107/S0909049510036009 Text en © Mikael Elias et al. 2011 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Diffraction Structural Biology
Elias, Mikael
Liebschner, Dorothee
Gotthard, Guillaume
Chabriere, Eric
Structural insights and ab initio sequencing within the DING proteins family
title Structural insights and ab initio sequencing within the DING proteins family
title_full Structural insights and ab initio sequencing within the DING proteins family
title_fullStr Structural insights and ab initio sequencing within the DING proteins family
title_full_unstemmed Structural insights and ab initio sequencing within the DING proteins family
title_short Structural insights and ab initio sequencing within the DING proteins family
title_sort structural insights and ab initio sequencing within the ding proteins family
topic Diffraction Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004253/
https://www.ncbi.nlm.nih.gov/pubmed/21169690
http://dx.doi.org/10.1107/S0909049510036009
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