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...
Autores principales: | , , , , , |
---|---|
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 |