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| Item Type: | Article |
|---|---|
| Title: | Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold |
| Creators Name: | Manjasetty, B.A., Buessow, K., Fieber-Erdmann, M., Roske, Y., Gobom, J., Scheich, C., Goetz, F., Niesen, F.H. and Heinemann, U. |
| Abstract: | The human protein PTD012 is the longer product of an alternatively spliced gene and was described to be localized in the nucleus. The X-ray structure analysis at 1.7 A resolution of PTD012 through SAD phasing reveals a monomeric protein and a novel fold. The shorter splice form was also studied and appears to be unfolded and non-functional. The structure of PTD012 displays an abba four-layer topology. A metal ion residing between the central b-sheets is partially coordinated by three histidine residues. X-ray absorption near-edge structure (XANES) analysis identifies the PTD012-bound ion as Zn2+. Tetrahedral coordination of the ion is completed by the carboxylate oxygen atom of an acetate molecule taken up from the crystallization buffer. The binding of Zn2+ to PTD012 is reminiscent of zinccontaining enzymes such as carboxypeptidase, carbonic anhydrase, and b-lactamase. Biochemical assays failed to demonstrate any of these enzyme activities in PTD012. However, PTD012 exhibits ester hydrolase activity on the substrate p-nitrophenyl acetate. |
| Keywords: | Alternative Splicing, PTD012 Family, Splice Variant, Structural Genomics, Zn-Binding Site, Ester Hydrolase, Animals |
| Source: | Protein Science |
| ISSN: | 0961-8368 |
| Publisher: | Cold Spring Harbor Laboratory Press |
| Volume: | 15 |
| Number: | 4 |
| Page Range: | 914-920 |
| Date: | 1 April 2006 |
| Official Publication: | https://doi.org/10.1110/ps.052037006 |
| PubMed: | View item in PubMed |
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