Cargando…

Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct

As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34 and 2.56 Å without a priori knowledge of the prot...

Descripción completa

Detalles Bibliográficos
Autores principales: Grøftehauge, Morten K., Truan, Daphne, Vasil, Adriana, Denny, Paul W., Vasil, Michael L., Pohl, Ehmke
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4519933/
https://www.ncbi.nlm.nih.gov/pubmed/26184183
http://dx.doi.org/10.3390/ijms160715971
_version_ 1782383582029807616
author Grøftehauge, Morten K.
Truan, Daphne
Vasil, Adriana
Denny, Paul W.
Vasil, Michael L.
Pohl, Ehmke
author_facet Grøftehauge, Morten K.
Truan, Daphne
Vasil, Adriana
Denny, Paul W.
Vasil, Michael L.
Pohl, Ehmke
author_sort Grøftehauge, Morten K.
collection PubMed
description As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34 and 2.56 Å without a priori knowledge of the protein identity or experimental phases. The three-dimensional structure of YcaC adopts a well-known cysteine hydrolase fold with the putative active site residues conserved. The active site cysteine is covalently bound to propionamide in one crystal form, whereas the second form contains an S-mercaptocysteine. The precise biological function of YcaC is unknown; however, related prokaryotic proteins have functions in antibacterial resistance, siderophore production and NADH biosynthesis. Here, we show that YcaC is exceptionally well conserved across both bacterial and fungal species despite being non-ubiquitous. This suggests that whilst YcaC may not be part of an integral pathway, the function could confer a significant evolutionary advantage to microbial life.
format Online
Article
Text
id pubmed-4519933
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-45199332015-08-03 Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct Grøftehauge, Morten K. Truan, Daphne Vasil, Adriana Denny, Paul W. Vasil, Michael L. Pohl, Ehmke Int J Mol Sci Article As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34 and 2.56 Å without a priori knowledge of the protein identity or experimental phases. The three-dimensional structure of YcaC adopts a well-known cysteine hydrolase fold with the putative active site residues conserved. The active site cysteine is covalently bound to propionamide in one crystal form, whereas the second form contains an S-mercaptocysteine. The precise biological function of YcaC is unknown; however, related prokaryotic proteins have functions in antibacterial resistance, siderophore production and NADH biosynthesis. Here, we show that YcaC is exceptionally well conserved across both bacterial and fungal species despite being non-ubiquitous. This suggests that whilst YcaC may not be part of an integral pathway, the function could confer a significant evolutionary advantage to microbial life. MDPI 2015-07-14 /pmc/articles/PMC4519933/ /pubmed/26184183 http://dx.doi.org/10.3390/ijms160715971 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Grøftehauge, Morten K.
Truan, Daphne
Vasil, Adriana
Denny, Paul W.
Vasil, Michael L.
Pohl, Ehmke
Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct
title Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct
title_full Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct
title_fullStr Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct
title_full_unstemmed Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct
title_short Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct
title_sort crystal structure of a hidden protein, ycac, a putative cysteine hydrolase from pseudomonas aeruginosa, with and without an acrylamide adduct
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4519933/
https://www.ncbi.nlm.nih.gov/pubmed/26184183
http://dx.doi.org/10.3390/ijms160715971
work_keys_str_mv AT grøftehaugemortenk crystalstructureofahiddenproteinycacaputativecysteinehydrolasefrompseudomonasaeruginosawithandwithoutanacrylamideadduct
AT truandaphne crystalstructureofahiddenproteinycacaputativecysteinehydrolasefrompseudomonasaeruginosawithandwithoutanacrylamideadduct
AT vasiladriana crystalstructureofahiddenproteinycacaputativecysteinehydrolasefrompseudomonasaeruginosawithandwithoutanacrylamideadduct
AT dennypaulw crystalstructureofahiddenproteinycacaputativecysteinehydrolasefrompseudomonasaeruginosawithandwithoutanacrylamideadduct
AT vasilmichaell crystalstructureofahiddenproteinycacaputativecysteinehydrolasefrompseudomonasaeruginosawithandwithoutanacrylamideadduct
AT pohlehmke crystalstructureofahiddenproteinycacaputativecysteinehydrolasefrompseudomonasaeruginosawithandwithoutanacrylamideadduct