1shn
From Proteopedia
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|PDB= 1shn |SIZE=350|CAPTION= <scene name='initialview01'>1shn</scene>, resolution 2.15Å | |PDB= 1shn |SIZE=350|CAPTION= <scene name='initialview01'>1shn</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1k7h|1K7H]], [[1ew2|1EW2]], [[1alk|1ALK]], [[1shq|1SHQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1shn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1shn OCA], [http://www.ebi.ac.uk/pdbsum/1shn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1shn RCSB]</span> | ||
}} | }} | ||
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[[Category: Lindley, P F.]] | [[Category: Lindley, P F.]] | ||
[[Category: McSweeney, S.]] | [[Category: McSweeney, S.]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: alkaline phosphatase]] | [[Category: alkaline phosphatase]] | ||
[[Category: beta sheet]] | [[Category: beta sheet]] | ||
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[[Category: zinc triad]] | [[Category: zinc triad]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:42:08 2008'' |
Revision as of 20:42, 30 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Alkaline phosphatase, with EC number 3.1.3.1 | ||||||
| Related: | 1K7H, 1EW2, 1ALK, 1SHQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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