1shn

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[[Image:1shn.gif|left|200px]]<br /><applet load="1shn" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1shn.gif|left|200px]]
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caption="1shn, resolution 2.15&Aring;" />
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'''Crystal structure of shrimp alkaline phosphatase with phosphate bound'''<br />
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{{Structure
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|PDB= 1shn |SIZE=350|CAPTION= <scene name='initialview01'>1shn</scene>, resolution 2.15&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]
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|GENE=
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}}
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'''Crystal structure of shrimp alkaline phosphatase with phosphate bound'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pandalus_borealis Pandalus borealis] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHN OCA].
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1SHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pandalus_borealis Pandalus borealis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SHN OCA].
==Reference==
==Reference==
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Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase., de Backer MM, McSweeney S, Lindley PF, Hough E, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1555-61. Epub 2004, Aug 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15333925 15333925]
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Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase., de Backer MM, McSweeney S, Lindley PF, Hough E, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1555-61. Epub 2004, Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15333925 15333925]
[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Pandalus borealis]]
[[Category: Pandalus borealis]]
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[[Category: zinc triad]]
[[Category: zinc triad]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:05:03 2008''

Revision as of 12:05, 20 March 2008

Image:1shn.gif


PDB ID 1shn

Drag the structure with the mouse to rotate
, resolution 2.15Å
Ligands: , , and
Activity: Alkaline phosphatase, with EC number 3.1.3.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of shrimp alkaline phosphatase with phosphate bound


Overview

Alkaline phosphatases (APs) are homodimeric metalloenzymes that catalyze the hydrolysis and transphosphorylation of phosphate monoesters. Each monomer contains a metal-binding triad that for optimal activity is usually occupied by two zinc ions and one magnesium ion. The recently determined crystal structure of cold-active shrimp alkaline phosphatase (SAP) was, however, fully occupied by zinc ions. This paper describes a metal-exchange experiment in which the zinc ion in one binding site (referred to as the M3 site) is replaced by magnesium. Crystal structures revealed a concomitant structural change: the metal exchange causes movement of a ligating histidine into a conformation in which it does not coordinate to the metal ion. The M3 site is relevant to catalysis: its occupation by magnesium is postulated to favour catalysis and it has been suggested to be a regulatory site for other APs. Further crystallographic studies show that ligand binding can induce a conformational change of an active-site arginine from a 'non-docked' (non-interacting) to a 'docked' conformation (interacting with the ligand). The first conformation has only been observed in SAP, while the latter is common in available AP structures. The observation that the arginine does not always bind the substrate may explain the increased catalytic efficiency that is generally observed for cold-active enzymes.

About this Structure

1SHN is a Single protein structure of sequence from Pandalus borealis. Full crystallographic information is available from OCA.

Reference

Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase., de Backer MM, McSweeney S, Lindley PF, Hough E, Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1555-61. Epub 2004, Aug 26. PMID:15333925

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