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Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold

Item Type:Article
Title:Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold
Creators Name:Manjasetty, B.A. and Buessow, K. and Fieber-Erdmann, M. and Roske, Y. and Gobom, J. and Scheich, C. and Goetz, F. and 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
Publisher:Cold Spring Harbor Laboratory Press
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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