1xcr
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(New page: 200px<br /> <applet load="1xcr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xcr, resolution 1.70Å" /> '''Crystal Structure o...)
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Revision as of 17:57, 12 November 2007
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Crystal Structure of Longer Splice Variant of PTD012 from Homo sapiens reveals a novel Zinc-containing fold
Overview
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 alphabetabetaalpha four-layer topology. A metal ion, residing between the central beta-sheets is partially coordinated by three, histidine residues. X-ray absorption near-edge structure (XANES) analysis, identifies the PTD012-bound ion as Zn(2+). 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 Zn(2+) to PTD012, is reminiscent of zinc-containing enzymes such as carboxypeptidase, carbonic anhydrase, and beta-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.
About this Structure
1XCR is a Single protein structure of sequence from Homo sapiens with ZN and ACY as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of Homo sapiens PTD012 reveals a zinc-containing hydrolase fold., Manjasetty BA, Bussow K, Fieber-Erdmann M, Roske Y, Gobom J, Scheich C, Gotz F, Niesen FH, Heinemann U, Protein Sci. 2006 Apr;15(4):914-20. Epub 2006 Mar 7. PMID:16522806
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