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Int. J. Mol. Sci. 2015, 16(7), 15971-15984; doi:10.3390/ijms160715971

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

1
School of Biological and Biomedical Sciences, Durham University, Durham DH1 3LE, UK
2
Swiss Light Source, Paul Scherrer Institute, Villigen CH-5232, Switzerland
3
Department of Immunology and Microbiology, University of Colorado School of Medicine, Aurora, CO 80045, USA
4
School of Medicine, Pharmacy and Health, Durham University, Stockton-on-Tees TS17 6BH, UK
5
Department of Chemistry, Durham University, Durham DH1 3LE, UK
Current address: Janssen Infectious Diseases and Vaccines, Archimedesweg 4-6, Leiden 2333CN, The Netherlands.
*
Authors to whom correspondence should be addressed.
Academic Editor: Charles A. Collyer
Received: 26 April 2015 / Revised: 4 June 2015 / Accepted: 15 June 2015 / Published: 14 July 2015
(This article belongs to the Special Issue Protein Crystallography in Molecular Biology 2015)
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Abstract

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. View Full-Text
Keywords: X-ray crystallography; micro-crystals; molecular replacement; YcaC; isochorismate family; protein octamer X-ray crystallography; micro-crystals; molecular replacement; YcaC; isochorismate family; protein octamer
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Grøftehauge, M.K.; Truan, D.; Vasil, A.; Denny, P.W.; Vasil, M.L.; Pohl, E. Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct. Int. J. Mol. Sci. 2015, 16, 15971-15984.

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