4wh0

YcaC from Pseudomonas aeruginosa with S-mercaptocysteine active site cysteine

spinqualitylabelsall models 4wh0, resolution 2.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wh0 is a 8 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.563Å Ligands: CL, CSS, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9I4D6_PSEAE Publication Abstract from PubMed 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 A 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. Crystal Structure of a Hidden Protein, YcaC, a Putative Cysteine Hydrolase from Pseudomonas aeruginosa, with and without an Acrylamide Adduct.,Groftehauge MK, Truan D, Vasil A, Denny PW, Vasil ML, Pohl E Int J Mol Sci. 2015 Jul 14;16(7):15971-84. doi: 10.3390/ijms160715971. PMID:26184183 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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