1xcr
From Proteopedia
(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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| - | [[Image:1xcr.gif|left|200px]]<br /> | + | [[Image:1xcr.gif|left|200px]]<br /><applet load="1xcr" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xcr" size=" | + | |
caption="1xcr, resolution 1.70Å" /> | caption="1xcr, resolution 1.70Å" /> | ||
'''Crystal Structure of Longer Splice Variant of PTD012 from Homo sapiens reveals a novel Zinc-containing fold'''<br /> | '''Crystal Structure of Longer Splice Variant of PTD012 from Homo sapiens reveals a novel Zinc-containing fold'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human protein PTD012 is the longer product of an alternatively spliced | + | 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== | ==About this Structure== | ||
| - | 1XCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XCR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Goetz, F.]] | [[Category: Goetz, F.]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
| - | [[Category: Manjasetty, B | + | [[Category: Manjasetty, B A.]] |
[[Category: Roske, Y.]] | [[Category: Roske, Y.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
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[[Category: zinc-containing fold]] | [[Category: zinc-containing fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:23 2008'' |
Revision as of 13:53, 21 February 2008
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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 and 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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