1ute
From Proteopedia
(New page: 200px<br /><applet load="1ute" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ute, resolution 1.55Å" /> '''PIG PURPLE ACID PHOS...) |
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| - | [[Image:1ute.jpg|left|200px]]<br /><applet load="1ute" size=" | + | [[Image:1ute.jpg|left|200px]]<br /><applet load="1ute" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ute, resolution 1.55Å" /> | caption="1ute, resolution 1.55Å" /> | ||
'''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''<br /> | '''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Mammalian purple acid phosphatases are highly conserved | + | BACKGROUND: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. RESULTS: The 1.55 A resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched beta sheets flanked by alpha-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. CONCLUSIONS: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design. |
==About this Structure== | ==About this Structure== | ||
| - | 1UTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with PO4, FEO and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http:// | + | 1UTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=FEO:'>FEO</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Guddat, L | + | [[Category: Guddat, L W.]] |
[[Category: Hamilton, S.]] | [[Category: Hamilton, S.]] | ||
[[Category: Hume, D.]] | [[Category: Hume, D.]] | ||
| - | [[Category: Jersey, J | + | [[Category: Jersey, J De.]] |
| - | [[Category: Martin, J | + | [[Category: Martin, J L.]] |
[[Category: Mcalpine, A.]] | [[Category: Mcalpine, A.]] | ||
[[Category: FEO]] | [[Category: FEO]] | ||
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[[Category: uteroferrin]] | [[Category: uteroferrin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:05 2008'' |
Revision as of 13:28, 21 February 2008
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PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE
Overview
BACKGROUND: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. RESULTS: The 1.55 A resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched beta sheets flanked by alpha-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. CONCLUSIONS: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design.
About this Structure
1UTE is a Single protein structure of sequence from Sus scrofa with , and as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of mammalian purple acid phosphatase., Guddat LW, McAlpine AS, Hume D, Hamilton S, de Jersey J, Martin JL, Structure. 1999 Jul 15;7(7):757-67. PMID:10425678
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