1ute

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[[Image:1ute.jpg|left|200px]]
[[Image:1ute.jpg|left|200px]]
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{{Structure
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|PDB= 1ute |SIZE=350|CAPTION= <scene name='initialview01'>1ute</scene>, resolution 1.55&Aring;
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The line below this paragraph, containing "STRUCTURE_1ute", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ute| PDB=1ute | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ute FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ute OCA], [http://www.ebi.ac.uk/pdbsum/1ute PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ute RCSB]</span>
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}}
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'''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''
'''PIG PURPLE ACID PHOSPHATASE COMPLEXED WITH PHOSPHATE'''
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[[Category: Martin, J L.]]
[[Category: Martin, J L.]]
[[Category: Mcalpine, A.]]
[[Category: Mcalpine, A.]]
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[[Category: metalloenzyme]]
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[[Category: Metalloenzyme]]
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[[Category: purple acid phosphatase]]
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[[Category: Purple acid phosphatase]]
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[[Category: tartrate resistant acid phosphatase]]
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[[Category: Tartrate resistant acid phosphatase]]
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[[Category: uteroferrin]]
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[[Category: Uteroferrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:39:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:15:01 2008''
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Revision as of 08:39, 3 May 2008

Template:STRUCTURE 1ute

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. 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 Page seeded by OCA on Sat May 3 11:39:48 2008

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