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Crystal structure of a hidden protein, YcaC, a putative cysteine hydrolase from Pseudomonas aeruginosa, with and without an acrylamide adduct.

Grøftehauge, M.K. and Truan, D. and Vasil, A. and Denny, P.W. and Vasil, M.L. and Pohl, E. (2015) 'Crystal structure of a hidden protein, YcaC, a putative cysteine hydrolase from Pseudomonas aeruginosa, with and without an acrylamide adduct.', International journal of molecular sciences., 16 (7). pp. 15971-15984.

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.

Item Type:Article
Keywords:X-ray crystallography, Micro-crystals, Molecular replacement, YcaC, Isochorismate family, Protein octamer.
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Status:Peer-reviewed
Publisher Web site:http://dx.doi.org/10.3390/ijms160715971
Publisher statement: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.
Date accepted:15 June 2015
Date deposited:04 September 2015
Date of first online publication:July 2015
Date first made open access:No date available

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