1xzw

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[[Image:1xzw.jpg|left|200px]]<br /><applet load="1xzw" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xzw.jpg|left|200px]]
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caption="1xzw, resolution 2.5&Aring;" />
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'''Sweet potato purple acid phosphatase/phosphate complex'''<br />
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{{Structure
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|PDB= 1xzw |SIZE=350|CAPTION= <scene name='initialview01'>1xzw</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Sweet potato purple acid phosphatase/phosphate complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XZW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ipomoea_batatas Ipomoea batatas] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=PO4:'>PO4</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=1XZW OCA].
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1XZW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ipomoea_batatas Ipomoea batatas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XZW OCA].
==Reference==
==Reference==
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Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase., Schenk G, Gahan LR, Carrington LE, Mitic N, Valizadeh M, Hamilton SE, de Jersey J, Guddat LW, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):273-8. Epub 2004 Dec 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15625111 15625111]
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Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase., Schenk G, Gahan LR, Carrington LE, Mitic N, Valizadeh M, Hamilton SE, de Jersey J, Guddat LW, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):273-8. Epub 2004 Dec 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15625111 15625111]
[[Category: Acid phosphatase]]
[[Category: Acid phosphatase]]
[[Category: Ipomoea batatas]]
[[Category: Ipomoea batatas]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:00:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:16:40 2008''

Revision as of 13:16, 20 March 2008

Image:1xzw.jpg


PDB ID 1xzw

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , and
Activity: Acid phosphatase, with EC number 3.1.3.2
Coordinates: save as pdb, mmCIF, xml



Sweet potato purple acid phosphatase/phosphate complex


Overview

Purple acid phosphatases (PAPs) are a family of binuclear metalloenzymes that catalyze the hydrolysis of phosphoric acid esters and anhydrides. A PAP in sweet potato has a unique, strongly antiferromagnetically coupled Fe(III)-Mn(II) center and is distinguished from other PAPs by its increased catalytic efficiency for a range of activated and unactivated phosphate esters, its strict requirement for Mn(II), and the presence of a mu-oxo bridge at pH 4.90. This enzyme displays maximum catalytic efficiency (k(cat)/K(m)) at pH 4.5, whereas its catalytic rate constant (k(cat)) is maximal at near-neutral pH, and, in contrast to other PAPs, its catalytic parameters are not dependent on the pK(a) of the leaving group. The crystal structure of the phosphate-bound Fe(III)-Mn(II) PAP has been determined to 2.5-A resolution (final R(free) value of 0.256). Structural comparisons of the active site of sweet potato, red kidney bean, and mammalian PAPs show several amino acid substitutions in the sweet potato enzyme that can account for its increased catalytic efficiency. The phosphate molecule binds in an unusual tripodal mode to the two metal ions, with two of the phosphate oxygen atoms binding to Fe(III) and Mn(II), a third oxygen atom bridging the two metal ions, and the fourth oxygen pointing toward the substrate binding pocket. This binding mode is unique among the known structures in this family but is reminiscent of phosphate binding to urease and of sulfate binding to lambda protein phosphatase. The structure and kinetics support the hypothesis that the bridging oxygen atom initiates hydrolysis.

About this Structure

1XZW is a Single protein structure of sequence from Ipomoea batatas. Full crystallographic information is available from OCA.

Reference

Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase., Schenk G, Gahan LR, Carrington LE, Mitic N, Valizadeh M, Hamilton SE, de Jersey J, Guddat LW, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):273-8. Epub 2004 Dec 29. PMID:15625111

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