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

Morten K. Grྏtehauge³  Daphne Truan²  Adriana Vasil¹  Paul W. Denny³  Michael L. Vasil¹  Ehmke Pohl³ 

[1] Department of Immunology and Microbiology, University of Colorado School of Medicine, Aurora, CO 80045, USA; E-Mails:;Swiss Light Source, Paul Scherrer Institute, Villigen CH-5232, Switzerland; E-Mail:;School of Biological and Biomedical Sciences, Durham University, Durham DH1 3LE, UK; E-Mail:

关键词: X-ray crystallography;    micro-crystals;    molecular replacement;    YcaC;    isochorismate family;    protein octamer;   

DOI  :  10.3390/ijms160715971

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.