1war

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[[Image:1war.gif|left|200px]]<br /><applet load="1war" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1war.gif|left|200px]]
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caption="1war, resolution 2.22&Aring;" />
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'''RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS'''<br />
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{{Structure
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|PDB= 1war |SIZE=350|CAPTION= <scene name='initialview01'>1war</scene>, resolution 2.22&Aring;
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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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'''RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1WAR 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=NAG:'>NAG</scene>, <scene name='pdbligand=FE:'>FE</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] Known structural/functional Site: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAR OCA].
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1WAR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAR OCA].
==Reference==
==Reference==
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Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop., Strater N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM, J Mol Biol. 2005 Aug 5;351(1):233-46. Epub 2005 Apr 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15993892 15993892]
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Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop., Strater N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM, J Mol Biol. 2005 Aug 5;351(1):233-46. Epub 2005 Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15993892 15993892]
[[Category: Acid phosphatase]]
[[Category: Acid phosphatase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: uteroferrin]]
[[Category: uteroferrin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:54:28 2008''

Revision as of 12:54, 20 March 2008


PDB ID 1war

Drag the structure with the mouse to rotate
, resolution 2.22Å
Sites:
Ligands: , and
Activity: Acid phosphatase, with EC number 3.1.3.2
Coordinates: save as pdb, mmCIF, xml



RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS


Overview

The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution. In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III). The main difference between the two structures is the conformation of the enzyme "repression loop". Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs. In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex. The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme. In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures. The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.

About this Structure

1WAR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop., Strater N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM, J Mol Biol. 2005 Aug 5;351(1):233-46. Epub 2005 Apr 26. PMID:15993892

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